(12) Patent Application Publication (10) Pub. No.: US 2008/ A1

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1 (19) United States US A1 (12) Patent Application Publication (10) Pub. No.: US 2008/ A1 Barget al. (43) Pub. Date: Mar. 27, 2008 (54) KERATIN-BINDING POLYPEPTIDES (30) Foreign Application Priority Data (75) Inventors: Heiko Barg. Speyer (DE): May 24, 2004 (DE) O Thomas Subkowski, Ladenburg Mar. 14, 2005 (DE) O (DE); Hans-Georg Lemaire, Publication Classification Limburgerhof (DE); Claus Bollschweiler, Heidelberg (DE): (51) Int. Cl. Arne Ptock, Ludwigshafen (DE) A61K 8/64 ( ) C07K I4/475 ( ) Correspondence Address: (52) U.S. Cl /70.14:530/350 CONNOLLY BOVE LODGE & HUTZ, LLP (57) ABSTRACT P O BOX 2207 WILMINGTON, DE (73) Assignee: BASF Aktiengesellschaft, Ludwigshafen (DE) (21) Appl. No.: 11/597,815 (22) PCT Filed: May 24, 2005 (86). PCT No.: PCT/EP05/05599 S 371 (c)(1), (2), (4) Date: Nov. 22, 2006 The invention relates to novel keratin-binding protein active Substances, and also to the production and use thereof. Particularly suitable keratin-binding polypeptides are sequences which are contained in human desmoplakin or are derived therefrom by altering the human desmoplakin polypeptide sequences such as amino acid insertions, Sub stitutions or deletions. The polypeptide sequences of the human desmoplakin is represented in SEQ ID NO: 1. A Suitable keratin-binding domain (domain B) is the polypep tide sequence SEQ ID NO: 1, position , in addition to functional equivalents thereof. An additional keratin-binding domain (domain C) is the polypeptide sequence SEQ ID NO: 1, position and the functional equivalents thereof.

2 Patent Application Publication Mar. 27, 2008 Sheet 1 of 27 US 2008/ A1 Figure 1 Protein alignment: Desmoplakin vs. Plectin Domain B Desmoplakin sequence hprod Plectinl - hrpd Desmoplakin sequence hprod Plectinl - hrpd Desmoplakin sequence hpra Plectinl - hrpd Desmoplakin sequence hprod Plectin) - hrpd Desmoplakin sequence hprod Plectinl - hrpd Desmoplakin sequence Plectin - Desmoplakin sequence Plectin - hprod hrpd hprod hrpd Desmoplakin sequence hpra Plectinl - hrpd Desmoplakin sequence Plectin - Desmoplakin sequence Plectin - Desmoplakin sequence Plectii - Desmoplakin sequence Plectin1 - hprod hrpd hprod hrpd hprd hrpd hprod hrpd Desmoplakin sequence hprod Plectin - hrpd Desmoplakin sequence hprod Plectinil - hrpd Desmoplakin sequence hprod Plectinl - hrpd (22O6) EPHGLLLSWOKRSM (3971) HDQLSEPSEVRSYVDPSTDERLSYTOLLKRCRRDDGSGOLLLPLSDARKL (2209) SFOGIROPVTvTELVDSGILRPSTVNELESGoISYDEVGERIKDFLQGSS (402). TFRGLRKOITMEELVRSOVM DEATALOLREGLTSEEVTKNLQKFLEGTS 2259 Domain B 2308 (2259) CIAGIYNETTKOKLGIYEAMKIGLVRPGTALELLEAQAATGFIVDPWSNL (4071) CIAGVFWDATKERLSVYQAMKKGIIRPGTAFELLEAQAATGYVIDPIKGL - (2309) RLPVEEAYKRGLVGIEFKEKLLSAERAVTGYNDPETGNIISLFQAMNKEL (4121) KLTVEEAVRMGIvGPEFKDKLLSAERAVTGYKDPYSGKLISLFQAMKKGL (2359). IEKGHGIRLLEAOIATGGIIDPKESHRLPVDIAYKRGYFNEELSEILSDP (471) ILKDHGIRLLEAQIATGGIIDPEESHRLPVEWAYKRGLFDEEMNEILTDP (2409) SDDTKGFFDPNTEENLTYLOKERCIKDEETGLCLIPLKEKKKOVOTSOK (4221) SDDTKGFFDPNTEENLTYLOLMERCITDPQTGLCLLPLKEKKRERKTSSK (2459). NTRKRRVVIVDPETNKEMSVQEAYKKGLIDYETFKELCEQECEWEEITI (427 l) SSWRKRRVVIVDPETGKEMSVYEAYRKGLIDHOTYLELSEOECEWEEITI (2509) TGSDGSTRVVLVDRKTGsoyDIQDAIDKGLVDRKFFDOYRSGSLSLTQFA ( 4321) SSSDGVVKSMIIDRRSGRQYDIDDAIAKNLIDRSALDQYRAGTLSITEFA (2559) DMISLKNGVGTSSSMGSGWSDDVFSSSRHESVSKISTISSWRNLTIRSSS (437l) DMLSGNAGGFRSRSSSVGSSSSYPISP AVSRTOLAS 2609 DOrnain C 2658 (2609) FSDTLEESSPIAAIFDTENLEKISITEGIERGIWDSITGQRLLEAQACTG (4407) WSDPTEETGPWAGILDTETLEKVSITEAMHRNLVDNITGQRLLEAQACTG O8 (2659) GIIHPTTGOKLSLQDAVSOGWIEODMATSWKPAOKAFIGFEGWKGKKKMS (4457) GIIDPSTGERLPVTDAVNKGLVDKIMVDRINLAQKAFCGFEDPRTKTKMS (2709) AAEAVKEKWLPYEAGQRFLE FOYLTGGLVDPEVHGRISTEEAIRKGFIDG (4507) AAQALKKGWLYYEAGORFLEVOYLTGGLIEPDTPGRVPLDEALQRGTVDA O8 (2759) RAAQRLQDTSSYAKILTCPKTKLKISYKDAINRSMVEDITGLRLLEAASW (4557) RTAOKLRDWGAYSKYLTCPKTKLKSYKDALDRSMWEEGTGIRLLEAAAQ (2809) SSKGLPSPYNMSSAPGSRSGSRSGSRSGSRSGSRSGSRRGS FDATGNSSY (4607) STKGYYSPYSWSGS GSTAGSRTGSRTGSRAGSRRGSFDATGSGFS (2859) SYSYSFSSSSIGH (4652) MTFSSSSYSSSGYGRRYASGSSASLGGPESAVA

3 Patent Application Publication Mar. 27, 2008 Sheet 2 of 27 US 2008/ A1 Figure 1 Total protein representation go EO 270 3ao) 4500 B Keratin-binding domain representation 41 Similarity Hill th lilah All parameter lilihilihilidh

4 Patent Application Publication Mar. 27, 2008 Sheet 3 of 27 US 2008/ A1 Figure 1 c=-s==== Translation of Desmoplakin 2872 aa Domain B Domain C

5 Patent Application Publication Mar. 27, 2008 Sheet 4 of 27 US 2008/ A1 Desmoplakin-Protein-Alignment Descoplakin human (NP_ ) (1) Unnamed Mus musculus (NP780547) (l) Plectin i Iso. 6 Mus musculus (NP ) (i) MWAGMLMPLDRRAIYEWLFREGWMVAKKDRRPRSLHPHVPGVTNLoVMR Sin. Plectin I human (AAHO7597) (l) Plectin 6 Rattus norvegicus (AAR95660) Plectin human (Q15149) (l) MVAGMLMPLDQLRAYEWLFREGVMVAKKDRRPRSLHPHVPGvTNIQVMR (1) MVAGMMPRDLRAYEWLPREGVMVAKKoRrpRSLHPHWPGVTNLOVMR Plectin l Iso. 5 human (NP ) (1) MWAGMLMPRDOLRAYEVFREGVMVAKKDRRPRSLPHWPGWTNLOVMR Plectin I Iso. lo human (NP958785) () S. 00 Desmoplakin human (NP ) (1) Unnamed Mus musculus (NP ) () r Plectin l Iso. 6 Mus musculus (NP ) (5) AMASLKARGIVRETFAWCHFYYLNEGIDHRQYLHLPPEIWPASLQRW Sin. Plectin I human (AAHO7597) (l) Plectin 6 Rattus norvegicus (AAR95660) (5) AMTSLKARGVRETFAWCHFYWYLTNEGIDHLRQYHLPPEIVPASLQRV Plectin l human (Q549) (5) AMASLRARGVRETFAWHFFWYTNEGIAHLRQYL.HLPPEIWAASLQRV Plectin l Iso. 6 human (NP958782) (sl) AMASLRARGIVRETFAWCHFYWYTNEGIAHLRQYHLPPEIWPASLQRW Plectin I Iso. 10 human (NP ) (i) Ol SO Desmoplakin human (NP ) () Unnamed Mus musculus (NP ) (i) Plectin l Iso. 6 Mus musculus (NP 95879l) (lol) RRPVAMVIPARRRSPHvomogPLGCPPKRGPLPAEDPAREERQVYRRKE Sin. Pectin human (AAHO7597) (1) Plectin 6 Rattus norvegicus (AAR95660) (lol) RRPVAMVMPARRRSPHVOTMQGPLGCPPKRGPLPAEDPAREERQVYRRKE Plectin l human (Q549) (lol) RRPVAMVMPARR-TPHvoAvogPLGsPPKRGPLPTEER LYRRKE Plectin Iso. 6 human (NP ) (Ol) RRPWAMVMPARR-TPHVAWQGPLGSPPKRGPLPTEEQR WYRrke Plectin I Iso. 10 human (NP ) (1) MSGAGGAFASPR OO Desmoplakin human (NP_ ) (l) r Unnamed Mus musculus (NP ) (l) Plectin i Iso. 6 Mus musculus (NP ) (lisl) REEGAPETPVVSATTweTLARPGPEPAPATDERDRvokkTFTKWVNKHLI Sin. Plectin. I human (AAHO7597) (1) Plectin 6 Rattus norvegicus (AARS5660) (l.51) REEGAPETPvwsATIwcTLARPGPEPTPATDERDRvokKTFTKWVNKHLI Plectin l human (ois 49) (145) LEEWSPETPVVPATTORTARPGPEPAPATDERDRWQKKTSTKwVNKHLI Plectin i Iso. 6 human (NP958782) (145) LEEVSPETPVVPATToRTLARPGPEPAPATDERDRVQKKTFTKWWNKHLI Plectin I Iso. 10 human (NP ) (3) -EWLLERPCNLDGGCEpARRGYYLCCVDERDRVOKKTFTKWWNKHL Desmoplakin human (NPO 04406) (1) Unnamed Mus musculus (NP ) (1) Plectin 3 Iso. 6 Mus musculus (NP ) (201) KAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIAL Sian. Plectin I human (AAHO7597) (1) Plectin 6 Rattus norvegicus (AARs5660) (201) KAQRHISDLYEDIRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNWOIA, Pectin human (Q1549) (195) KAORHISDYEDIRDGHNLISLLEWSGDSLPREKGRMRFHKQNVQAL Plectin l Iso. 6 human (NP ) (95 KAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIAL Plectin I Iso. 10 human (NP958785) (62) KAQRHISDLYEDLRDGHNLISLLEWLSGEDSLPREKGRMRFHKLQNVQIAL Desmoplakin human (NPoo4406) (l) Unnamed Mus musculus (NP ) (1) Plectin l iso. 6 Mus musculus (NP ) (251) Sitn. Plectin I human (AAHO7597) (l) Plectin 6 Rattus norvegicus (AAR95660) (251) DYLRHRQWKLVNIRNDDIADGNPKLTLGLIWTIIIHFQISDIQVSGQSED Plectin human (Q5149) (24s) DYLRHRQvKLVNIRNDDIADGNPKLTLGLI WTIILHFQISDIQVSGQSED Plectin i Iso. 6 human (NP958782) (245) DYLRHRQWKLVNIRNDDIADGNPKLTLGLIWTIIIHFQISDIQVSGoSED lectin I Iso. O human (NP958785) (ill2) DYLRHRQvKLVIRNDIADGNPKLTLGLIWTIILHFQISDIQvsGQSED 30 3SO Desmoplakin human (NP_ ) (1)

6 Patent Application Publication Mar. 27, 2008 Sheet 5 of 27 US 2008/ A1 Unnamed Mus musculus (NP ) (l) Plectin l Iso. 6 Mus musculus (NPS58791) {30) MTAKEKLLWSQRMVEGYOGLRCDNFTTSWRDGRFAIIHRHKPMLIDM Sita. Plectin human (AAHO7597) (i) r r Plectin S Rattus norvegicus (AAR95660) (30) MTAKEKLLWSQRMVEGYOGLRCDNFTTSWRDGRIFNAHRHKPMIDM Plectin human (Qls49) (29s) MTAKEKLLLWSQRMVEGYGLRCDNFTSSWRDGRLFNAIHRHKPLLIDM Plectin Iso. 6 human (NP ) (295) MTAKEKLLLWSORMVEGYOGLRCDFTsSWRGRLFNAHRHKPLLIDM Plectin I. Iso. i0 human (NP ) (62) MTAKEKLLIWSQRMVEGYGLRCDNFTssWRDGRNAEIHRHKPLLIOM

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8 Patent Application Publication Mar. 27, 2008 Sheet 7 of 27 US 2008/ A1 Figure 2 - a - Desmoplakin-Protein-Alignment Desinoplakin human (NP ) (70) GGYTCOSGSGWDRPTKHVTSECLGWMRQQRAEMDMVAWGVDLASVEQHIN Unnamed Mus musculus (NP ) (l) Plectin Iso. 6 Mus musculus (NP95879) (647) TLCSTORRPELEOSTLRYLQDLLAWWEENORRIDSAEWGWDLPSWEAQLG Sin. Plectin I hulaan (AAHO7597) (l) Plectin 6 Rattus norvegicus (AAR95660) (648) TLOSTORRPELEDSTLRYHDLLAWWEENQRRIDGAEWGVoIPSVEARLG Plectin human (Qls349) (644) rosvorrpeledstrylodllawweenorwdgaewgvlpsveaog Plectin l Iso. 6 human (NP958782) (644) TiOSVORRPEEDSTLRYLODAWWEENQHRVOGAEWGWDLPSVEAQLG Plectin I Iso. lo human (NP958785) (sl) TLQSvoRRPELEOSTLRYODLAWVEENOHRWDGAEWGWDLPSWACLG 70 so Desmoplakin human {NP_ ) 220) SHRGIHNSIGDYRWOLDKIKAOLREKS AIYOLEEEYENLK Unnamed Mus musculus (NP ) () Plectin i Iso. 6 Mus musculus (NP ) (697) Sim. Plectin human (AAHO7597) (l) Plectin 6 Rattus norvegicus (AAR95660) (698) SHRGMHQSEEFRAKERARNDESQLSPATRGAYROCLGRLDQYAKLLN Plectin i human (Q549) (694). SHRGLHQSIEEFQAKIERARSDEGQLSPATRGAYRDCLGRLDLOYAKLN Plectin i Iso. 5 human (NP ) (694). SHRGLHSIEEFRAKIERARSDEGQLsPARGAYRDCLGRLDLQYAKLLN Plectin I Iso. lo human (NP ) (56l) SHRGLHSIEEFRAKEERARSDEGOSPATRGAYRCLGRLDLOYAKLLN Desmoplakin human (NPOO4406) (2si). ASFERMDHLRQLONIEQATSREIMWINDCEEEELLYDWSDKNTNIAQKQE Unnamed Mus musculus (NP ) () Plectin so. 6 Mus musculus (NP 95879) (747). SSKARLRSLESLHGFWAAATKEMWLNEKEEEEWGFDWSORNTNMAAKKE Sim. Plectin I human (AAHO7597) (l) Plectin 6 Rattus norvegicus (AAR95660) (748) SSKARRSLESHGFWAAATKELMWLNEKEEEEWGFWSDRNTNMAAKKE Plectin human (Qlsl49) (744). SSKARRSLESHSFWAAATKEMWNEKEEEEWGFDWSDRNTNMTAKKE Plectin l Iso. 6 human (NPS58782) (744) isskarlrsleslhsfvaaatkelmwlnekeeeevgfdwsdrntnmtakke Plectin I Iso. lo human (NP ) (6) SSKARLRSLESHSFVAAATKEMWLNEKEEEEWGFDWSDRNTNMTAKKE SOL BSO Desmoplakin human (NP_ ) (3ll) AFSIRMSQLEVKEKELNKKQESDOLVNOHPASDKIEAYMOTOTQWSW Unnamed Mus musculus (NP ) (l) Plectin so. 6 Mus musculus (NP ) (797) SYSALMRELEMKEKKKEQNTGDRLREDHPARPTVESFQAALTQWSW Sim. Plectin I human (AAHO7597) (l) Plectin 5 Rattus norvegicus (AARS5660) (798) SYSAMRELEMKEKKIKEQNTGDRLLREDHPARPTVESFQAALQTOWSW Plectin i human (Q1549) Plectin l Iso. 6 human (NP958782) Plectin I Iso. lo human (NP 9587Bs) Desmoplakin human (NP ) (794) sysaimreelkekkikelonagdrllredhparptvesfqaalotowsw (794) SYSALMRELELKEKKIKELQNAGDRLLREDHPARPTVESFQAALOTQWSW (661) SYSALMRELELKEKKIKELQNAGDRILREDHPARPTVESFOAALOTQWSW (36) ELQITKCIDVHLKENAAYFQFFEEAQSTEAYLKGLQDSIRKKYPCDKNMP Unnamed Mus musculus (NP ) (l) Plectin l Iso. 6 Mus musculus (NP ) (847). MLQLCCCIEAHLKENTAYFQFFSDVREAEEQLQKLQETLRRKYSCDRTIT Sin. Plectin I human (AAHO7597) (i) Plectin 6 Rattus norvegicus (AARS5660) (848) MLQLCCCIEAHKENTAYFQFFSDWREAEEQLQKLQETLRRKYSCDRST Plectin human (Qls49) (844) MILCCCEAHLKENAAYFQFFSDVREAEGOLQKLQEALRRKNSCDRSAT Plectin l Iso. 6 human (NP ) (844) MLQL.cccIRAHLKENAAYFQFFSDVREAEGQLQKLQEALRRKYSCDRSAT Plectin I. Iso. 10 human {NP ) (711) MLQLCCCIEAHLKENAAYFQFFSDVREAEGQLQKLQEALRRKYSCDRSAT Desmoplakin human (NP_ ) (4li) LOHLLEQIKELEKEREKILEYKRQVONLVNKSKKIVQLKPRNPDYRSNKP Unnamed Mus musculus (NP ) () Plectin i Iso. 6 Mus musculus (NP ) (897) VTRLEDLIQDAQDEKEQLNEYKGHLSGLAKRAKAIVQLKPRNPAHPVRGH Sitn. Plectin. I human (AAHO7597) () Plectin 6 Rattus norvegicus (AAR95660) (898) WTRLEDLIQDAQDEKEQLNEYKGHISGLAKRAKAIVQLKPRNPAHPVRGH Plectin human (Qlsl49) (894) WTRLEDLLQDAQDEKEQLNEYKGHESGLAKRAKAWOLKPRHPAHPMRGR Plectin l Iso. 6 human (NP ) (894) wtrledliqdaqdekeqlneykghlsglakrakawwlkprhpahpmrgr Plectin I Iso. i0 human (NP ) (761) wtrledllodaqdekeqlneykghlsgakrakavvolkprhpahpmrgr

9 Patent Application Publication Mar. 27, 2008 Sheet 8 of 27 US 2008/ A1 9S Desmoplakin human (NPL ) 46l ELRAcDYKQQKEWHKGELKONNERSKYWTGPGGVoMLVPSWGL. Unnamed Mus musculus (NP780547) (l) Plectin i Iso. 6 Mus musculus (NP 95879) (94.7) WPLIAVODYKoVEVTVHKGoocoLVGPAOPSHWKVLSGSssEAAVPSwcF Sin. Plectin. I hunan (AAHO7597) (l) Plectin S Rattus norvegicus (AAR95660) (948) WPLLAVCOYKQVEVTVHKGoocQLVGPAQPFHWKVGGSSSAAVPSWCP Pectin human (Q549) (944) LPLLAWCDYKOWEVTVHKGDECQLVGPAQPSHWKVLSSSGSEAAVPSWCF Plectin l Iso. 6 human (NP958762) 944) LPLLAVODYKVEVTVHKGDECOLVGPAOPSHWKVLsssGSEAAVpsvcF Plectin I Iso. 10 human (NP ) (Bl) LPLIAVCDYKoVEVTVHKGDECQLVGPAQPSHWKVLSSSGSEAAVPSVCF OOl OSO Desmoplakin human (NP o ) 5ii) IPPPNPLAVDISCKEYYRAILALWNQLYINMKSLVSWHYCMIDIEK Unnamed Mus musculus (NP ) (i) Plectin l Iso. 6 Mus musculus (NP ) (997) VPPPNQEAQEAVARLEAQHQAVTLWHQLVDMKSLAWQSSRDIQL Sim. Pectin I human (AAHO7597) (1) Plectin 6 Rattus norvegicus (AAR95660) (998) LVPPPNOEAQEAVARLsAOHOALVTLWHOLHVDMKSLLAWOSLNRDIOLI Plectin l human (Qlsl49) (ssg.) IVPPPNQEVOEAVTRLEAQHQAVTLWHOVDMKSLAWQSLRRDVQLI Plectin l Iso. 6 human (NP9s 8782) (.994) LVPPPNQEAQEAWTRLEAQHCALVTLWHQLHWDMKSLLAWQSLRRDVQLI Plectin I Iso. O human (NP958785) (86 LVPPPNQEAQEAVTRLEAQHQALVTLWHQLHVDMKSLIAWQSLRRDVOLI OS OO Desmoplakin human (NP_ ) (56l) RAMTIAKLKTMRQEDYMKTALELHYQEFIRNSQGSEMFGDODKRKIQS Unnamed Mus musculus (NP ) (l) Plectin i Iso. 6 Mus musculus (NP ) (0.47) RSWSLWTFRTLKPEERQALRNLELHYQAFLRDSQDAGGFGPEDREVAER. Sim. Plectin I human (AAHO7597) (l) Plectin 6 Rattus norvegicus (AAR95660) (1048) RSWSLWTFRTLKPEEQRQARNLELHYQAFROSQDAGGFGPEDREWAER Plectin human (Qisl49) (1044) rswslatfrtlkpeeqrqalhslelyoafrdsoaggfgpedremaer Plectin Iso. 6 human (NP ) (log 4 RSWSLATFRTLKPEEQRALHSLELHYoAFLRDSQDAGGFGPRDRLMAER Plectin I Iso. 10 human (NP ) (9ll RSWSLATFRTLKPEEQRQALHSLELEYQAFROSQDAGGFGPEDRLMAER Ol SO Desmoplakin human (NP_ ) (61) QFTDAQKHYQTLVIQLPGYPOHOTWTTTEITHHGTCODVNHNKVIETNRE Unnamed Mus musculus (NP ) (l) Plectin i Iso. 6 Mus musculus (NP ) (1097) EYGSCSRHYQQLLQSLE OGEQ Sin. Plectin I human (AAHO7597) (l) Plectin 6 Rattus norvegicus (AARS5660) (los B} EYGSCSRHYQRLLSLE GEQ Plectin i human (Qlsi49) (los4) EYGSCSHHYQQLOSLE QGAQ Plectin l Iso. 6 human (NP958782) Plectin I Iso. 10 human (NP ) Desmoplakin human (NP_ ) (1094) EYGSCSHHYQQLLQSLE QGAO (961) EYGSCSHHYQQLLOSLE QGAQ (661) NDKQETWMLMELQKIRRQIEHCEGRMTLKNLPLADQGSSHHIVKINELK Unnamed Mus musculus (NP ) (l) Plectin l Iso. 6 Mus museulus (NP ) OOO (lili B) EESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKDPARECAQRIAEQQ Sim. Pectin I human (AAHO7597) () Plectin 6 Rattus norvegicus (AAR95660) (lil 9) EESRCORCISELKDIRLoLEACETRTVHRLRLPLDKDPARECAQRIAEQQ Plectin human (Cl549) (lii.5) EESRCQRCISELKDIRLQLEACETRTVHRRLPLDKEPARECAQRIAEQQ Plectin i Iso. 6 human (NP958782) (1115) EESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQRIAEQQ Plectin I Iso. 10 human (NP958785) (982) EESRCRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQRIAEQQ Desmoplakin human (NPOO4406) (7il) SWONDSQAIAEWLNQLKDMLANFRGSEK YCYLQNEWFGLFOKLENI Unnamed Mus musculus (NP ) (1) Plectin l Iso. 6 Mus musculus (NP ) (lisb) KAQAEWEGLGKGWARLSAEAEKVLALPEPS PAAPTLRSELELTLGKLEQV Siim. Plectin. I human (AAHO7597) (i) Plectin 6 Rattus norvegicus (AAR95660) (lié9) KAQAEVEGLGKGVARLSAEAEKVLALPEPSPAAPTLRSELELTLGKLEQV Plectin l human (Qls149) (lé5) KAQAEVEGLGKGWARLSAEAEKVLALPEPSPAAPTLRSELELTLGKLEQW Plectin l Iso. 6 human (NP958782) (less) KAQAEVEGGKGWARLSAEAEKVALPEPSPAAPTLRSELETLGKLEQV Plectin I Iso. lo human NP ) KAQAEVEGLcKGWARLSAEAEKVLALPEPSPAAPTLRSELELTLGKLEQV

10 Patent Application Publication Mar. 27, 2008 Sheet 9 of 27 US 2008/ A1 l2s 300 Destroplakin human (NP ) (757). NGVTDGYLNSLCTVRALLCALOTEDMLKVYEARLTEEETWCLDLDKVEA Unnamed Mus musculus (NP ) () Plectin i Iso. 6 Mus musculus (NPs 5879l) (a28) RSLSAIYLEKLKTISLVIRSTOGAEEVLKTHEEQLKEAQAVPATLQELEA Sin. Pectin. I human (AAHO7597) () Plectin 6 Rattus norvegicus (AAR95660) (29) RSLsAYLEKLKTISLVIRSTOGAEWLKTHEEHLKEAAVPATOEIEW Plectin human (Ql549) (las) RSSAYLEKKTISLVIRGTOGAEEWLRAHEEQLKEAQAVPATPELEA Plectin Plectin I. Iso. 6 human (NP ) Iso. 10 human (NP958785) (215) RSLSAIYLEKLKTISLVIRGTOGAEEVLRAHEEQLKEAQAvPATLPELEA (1082) RSLSAIYLEKLKTISLVIRGTOGAEEVLRAHEEQLKEAQAvPATLPELEA 30 3SO destinoplakin human (NP_ ) 807) YRCGLKKIKNDLNLKKSLLATMKELOKAQoIHSOTSCOYPLYDLDGKF Unnamed Mus musculus (NP ) (l) Plectin i Iso. 6 Mus musculus (NP95879) (268) reaslkklraqaeaoopvfntlrdergaqevgerlqqrhgerdveverw Sin. Plectin I human (AAHO7597) () Plectin 6 Rattus norvegicus (AAR9566O) (269) TKASLKKLRAQARAQOPwFNTLRDELRGAQEVGERLOORHGERDVEVERW Plectin l human (Osq9) (265). TKASLKKLRAQAEAQQPTFDARDERGAQEWGERLQQRHGEROVEVERW Plectin i Iso. 6 human (NP958782) (26s) TKASLKKLRAQAEACQPTFDALRDERGAQEVGERLOORHGERDWEVERW Plectin I Iso. i0 human (NP958785) (il32) TKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERW 3S 4 OO Desmoplakin human (NP ) (es) GrcKVTOLTDRWORDKODFRLWDLEKOIKQLRNYRDNYOAFCKWLYork Unnamed Mus musculus (NP ) (l) Plectin l Iso. 6 Mus musculus (NP95879) (318) RERVTOLLERWOAVLAOTDVRQRELEQLGRQLRYYRESADPLSAWLQDAK Sim. Plectin I human (AAHO7597) (l) Piectin 6 Rattus norvegicus (AAR ) (.319) RERVTOLLERWOAVACTDWRQRELECGROLRYYRESADPLSSWODAK Plectin l human (Qlsles) (315) RERWALIERWQAVLAQTIDWRQRELEQLGRQLRYYRESADPLGAWLQDAR Plectin l Iso. 6 human (NP958782) Plectin I Iso. 10 human (NP958785) (3ls) RERVAQLLERWAVLAQTDVRORELECLGRQLRYYRESADPLGAwl coar (lis2) RERVAQLLERWQAVLACTDVRQRELEQLGRQLRYYRESADPGAWLQDAR desinoplakin human (NP_ ) (907) RRQDSLESMKFGDSNTVMRFLNEQKNLHSEISGKRDKSEEWOKIAELCAN Unnamed Mus musculus (NP ) (l) Plectin l Iso. 6 Mus musculus (NP ) (1368) RRQEQIQAWPIANCOAAREQLROEKALLEEIERHGEKVEECQKFAKOYIN Sitn. Plectin I human (AAHO7597) (l) Plectin 6 Rattus norvegicus (AAR95660) (1369) SRCEQIQAVPIANSOAAREQLRoeKALLEEIERHGEKVEECQKFAKQYIN Plectin l human (Q549) (.365). RRREQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYIN Plectin l Iso. 6 human (NP958782) Plectin I Iso. O human (NP958785) (i365) RRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECORFAKQYIN (232) RRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYIN 45. SOO Desmoplakin human (NP_ ) (957) SIKDYELOLASYTSGLETLLNIPIKRTMIOSPSGWILOEAADVHARYIEL Unnamed Mus musculus (NP ) (l) Plectin l Iso. 6 Mus musculus (NP ) (1418) AIKDYELQLITYKAQLEPVASPAKK-PKVQSGSESVIQEYVDLRTRYSEL Sin. Plectin I human (AAHO7597) (l) Plectin 6 Rattus nor vegicus (AAR95660) 1419) AIKYEOLITYKAOLEPVASPAKK-PKWOSGSESVIQEYVDLRTRYSE Plectin in Plectin l human (Qls149) Iso. 6 human (NPL958782) (45) AIKDYELOLVTYKAOLEPVASPAKK-PKWQSGSESVIQEYVDLRTHYSEL (145) AIKDYELowrykAOLEPVASPAKK-PKWOSGSESWIOEYVDLRTYSE, Plectin I Iso. 10 human (NP958785) (1282) AIKDYELQLvTYKAQLsPVASPAKK-PKVQSGSESVIQEYVDLRTHYSEL SO 550 Desmoplakin human (NP_ ) (1007) LTRSGDYYRFLSEMLKSLEDLKLKNTKIEVLEEELRLARDANSRN Unnamed Mus musculus (NP ) (l) Plectin l Iso. 6 Mus musculus (NP ) (1467) TTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLA Sitn. Plectin I hullaan (AAHO7597) () Plectin 6 Rattus norvegicus (AARs5660) (l468) TTLTSQYIKFISETLRRMEEEERLAEOORAEERERAEVEAALEKORCLA Plectin l human (Qlsl49) (46.4) TTLTSQYIKFISETLRRMEBEERLAEQQRAEERERLAEVEAALEKQRQLA Plectin l Iso. 6 human (NP ) Plectin I. Iso. 10 human (NP ) (.464) TTLTSQYIKFISETLRRMEEEERIAEQORAEERERLAEVEAALEKQRQL.A (l33l) TTLTSQYIKFISETLRRMEEEERLAEOORAEERERLAEWEAALEKQROLA

11 Patent Application Publication Mar. 27, 2008 Sheet 10 of 27 US 2008/ A1 Desmoplakin human (NP_ ) (1052) Unnamed Mus musculus (NP ) Plectin l Iso. 6 Mus musculus (NP 95879) () (1517) Sin. Plectin I human (AAHO7597) () Plectin S Rattus norvegicus (AAR95660) (158) EAHAQAKAQAELEARELQRRMQEEVTRREEAAVEDAQQQKRSIQEELQHLR Plectin l human (Q549) (54) EAHAQAKAQAERRAKELOORQEEVVRREEAAVDAQOCKRSIOEELOOLR Plectin i Iso. 6 human (NP ) (1514) EAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLR Plectin I Iso. 10 human (NP ) (1381) EAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLR Desmoplakin human (NP_ ) (1052) CNKNKFLDONLQ KYOAECSQFKAKLASLEELKRQAELDGK Unnamed Mus musculus (NP ) (l) Plectin l Iso. 6 Mus musculus (NP 95879) (1567) QSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELO Sin. Plectin I hunan (AAHO7597) (l) Plectin 6 Rattus norvegicus (AAR95660) (1568) QSSEAEIQAKAQQWEAAERSRMRIEEEIRVWRIQLETTERQRGGAEDELQ Plectin l human (Qi549) (1564) QSSEAEIQAKARQAEAAERSRLRIEEERVVRLQLRATERQRGGAEGELQ Plectin i Iso. 6 human (NP958782) (1564) QSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQ Plectin I Iso. 10 human (NP958785) (1431) QSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQ Desmoplakin human (NP ) (1092) SAKQNLDKCYGQIKELNEKITRLTYEIEDE---KR R Unnamed Mus musculus (NP ) (i) r Plectin l Iso. 6 Mus musculus (NP95879l) (1617) ALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAR Sin. Plectin I human (AAHO7597) (l) Plectin 6 Rattus norvegicus (AAR95660) (lisi B) ALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAE Plectin i human (ols149) (64) ALRARAEEAEAOKRAEEAERRRVDESCRKRAEVELASRVKAEAE Plectin l Iso. 6 human (NP ) Plectin I Iso. 10 human (NP ) (isl4) ALRARAEEAEAQKRQAQEEAERLRRQWQDESQRKRQAEVELASRVKAEAE (1481) ALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAE Ol SO Desmoplakin human (NP_ ) (il 25) Unnamed Mus musculus (NP ) {1} Plectin 1. Iso. 6 Mus musculus (NP ) (1667) AAREKQRALQALDELRLQAEEAERRLRQAEAERARQVOVALETAQRSAEV Sim. Plectin I human (AAHO7597) (l) r r Plectin 6 Rattus norvegicus (AAR95660) Plectin l human (QlS149) (lé68). AAREKQRALQALDELKLQAEEAERRLRQAEAERARQWQVALETAORSAEV (664) AAREKQRALQALEELRLQAEEAERWLCQAEVERAROWVALETAQRSAEA Plectin i Iso. 6 human (NP ) Plectin I Iso. 10 human (NP ) (1664) AAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEA (1531) AAREKQRALQALEELRLQAEEAERRLRQAEVERARQVOVALETAQRSAEA 75 bod Desmoplakin human (NP ) (125) RK--SWEDRFDOQKN Unnamed Mus musculus (NP780547) (l) r -- Plectin l Iso., 6 Mus ausculius (NP ) (177). RISKRASFAEKTAOLERTLQEEHVTWAQLREEAERRAQQQAEAERAREE Sin. Plectin I human (AAHO7597) () Plectin 6 Rattus norvegicus (AARS5660) Plectin l human (Qlsl49) (1718) ELQSKRASFAEKTAQLERTLEEHWIWTQREEAERRAQQQAEAERAREE (1714) ELQSKRASFAEKTAOLERSLQEEHWAVAQLREEAERRAQQQAEAERAREE Plectin l Iso. 6 human (NP958782) Plectin I Iso. i0 human (NP958785) (1714) ELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREE (1581) ELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREE i Desmoplakin human (NP ) (ll 38) DYDQLQKARQCEKENLGWQKLESEKAIK Unnamed Mus musculus (NP ) (l) Plectin 1. Iso. 6 Mus musculus (NP95879) (1767) AERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRR Sin. Plectin. I hunara AAH07597) (1) Plectin 6 Rattus nor vegicus (AAR95660) (1768). AERELERWOLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRR Plectin l human (Qisl49) (764). AERQLERWQLKANEALRLRLQAEEWLookSLAQAEAEKQKEEAEREARRR Plectin l Iso. 6 human (NP958782) (1764) AERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRR Plectin I Iso. 10 human (NP ) (1631) AERELERWQLKANEALRLRLQAEEVAQOKSLAQAEAEKQKEEAEREARRR

12 Patent Application Publication Mar. 27, 2008 Sheet 11 of 27 US 2008/ A1 3S 90 ils 6) r - r s - s--k-eyeibrlrvlloeegtrkreyenelakvrnhyn--- Desroplakin human (NPO 04606) tinnamed Mus musculus (NP-7B 0547) () Plectin l Iso. 6 Mus musculus (NP95879) (sl) GKAEEAVRRELAEce.EKRAEGTAccra AEELIRLRAETEge Sin. Plectin human (AAHO7597) (l) r rr - - Plectin 6 Rattus nor vegicus (AAR95660) (lel 8) GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRIAAEQELIRLRAETEQge Plectin l human (QlS49) le4) GRAEEQAWRQRELAEQELEKQRLAEGTAORLAAEQELIRRAETECGE Plectin i Iso. 5 human (NP958782) { l8l4) GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGE Plectin I Iso. O human (NP ) l68l) GKAEEQAVRQRELAEQELEKORQLAEGTAQORLAAEOELIRLRAETEOgE ls Cl 950 Desmoplakin human (NP ) (laol) EEMSLRNKYTs Unnamed Mus musculus (NP ) (1) Plectin l Iso, 6 Mus musculus (NP ) is 67) QQRQLLEEELARLoHEATAATGKROERAEAKVRAEMEVILASKARAEE Sin. Plectin I human (AAHO7597) () Plectin 6 Rattus nor vegicus (AARs5660) (1868) QQROLLEEELARLQHEATAATOKRQELEAEEAKVRAEMEVLLASKARAEE Plectia hurrar (Ols. 49) (864) QQRQLLEEELARLQREAAAATQKRQELEAEAKVRAEMEWLLASKAKAEE Plectin l IBo. 5 human (NP ) (1864) QQRQLLEEELARLOREAAAATOKRQELEAELAKVRAEMEVLLASKARAEE Plectin I Iso. 1d human (NP ) (1731) QQRQLLEEELAREQREAAAATOKRQELRAEEAKVRAEMEVLLASKARAES iss 2000 Desmoplakin human (NP_ ) (1215) NITKTTIKEIS M Unnamed Mus musculus (NP ) (l) Plectin Iso. 6 Mus musculus (NP ) (1917) ESRSTSEKSKQRLEARAGRFRELAEEAARLRALAREAKRQRQLAEEDAAR Sin. Plectin. I human (AAHO7597) (l) Plectin 6 Rattus norvegicus (AAR95660) Plectin i human (Q1549) Plectin l Igo. 6 human (NP ) Plectin I Iso. 10 human (NP ) Desmoplakin human (NPOO44O6) 9l8) ESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRIAEEDAAR (94} ESRSTSEKSKQRLEAEAGRFRELAERAARLRALAEEAKRORQL.AEEDAAR l914) ESRSTSEKSKOREAEAGRFRELAEEAARLRALAEEAKRQRQAEEDAAR (l781) ESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQROLAEEDAAR 2Ol 2OSO (1227) QKEDDSKNLRNOLDRLSRENRDLKDEIVRLNDSILOATEORRRAEENALQ Unnamed Mus musculus (NP ) (1) Plectin l Iso. 6 Mus musculus (NPs 58791) (967). QRAEAERVLTEKLAAISEATRIKTEAEIALKEKEAENERRRLAEDEAFO Sim. Plectin human (AAHO7597) () r Plectin 6 Rattus norvegicus (AAR9566D) (1968 QRAEAERWITEKAASEATRKTEAEAKEKEAENERRRLAEDEAFO Plectin i human (Qls149) (lss4} QRAEAERVLAEKEAAGEATRLKTEAEIALKEKRAENERRRLAEDEAFO Plectin l Iso. 6 human (NP958782) Plectin I Iso. 10 human (NP ) (1964) QRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQ (le3l) QRAEAERVLAEKLAAIGEATREKTEAEIALKEKEAENERLRRLAEDEAFO 20S 200 (277) QKACGSEIMQKKQHLEIELKQVMQorse DNARHKOSLEEAAKTIQDKNKE Desmoplakin human (NP_ ) Unnamed Mus musculus (NP ) 1) Plectin l Iso. 6 Mus musculus (NP ) (207) RRRLEEQAALHKADIEERLACLRKASESELERQKGLVEDTLRORROWEEE Sin. Plectin human (AAHO7597) (l) Plectin 6 Rattus norvegicus (AAR95660) (2018) RRRLEEQAAQHKADIEERLAOLRKASESELERQKGLVEDTLRQRROVEEE Plectin l human (Q1549) (2014) RRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQWEEE Plectin l Iso. 6 human (NP ) (2014) RRRLEEQAAQHKADEERLAQLRKASDSELEROKGIVEDTLRQRROVEEE Plectin I Iso. O human (NP ) (881). RRRLEEQAAQHKADIEERLAQLRKASDSEERQKGLVEDTLRQRRQVEEE 2O 250 Desmoplakin human (NP_0044O6) (1327) IERLKAEFQEEAKRRWEYENELSKVRNNYDEEIISLKNQFETEINITKTT Unnamed Mus musculus (NP ) (l) w Plectin Iso. 6 Mus musculus (NP ) (2067) IMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLA Sim. Plectin I human (AAHO7597) (l) Plectin 6 Rattus nor vegicus (AAR95660) (2068} IMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQEAARQRQLA Plectin l human (Q1549) (2064.) ILALKASFEKAAAGKAELELELGRIRSNAEDTIRSKEQAELEAARQRQLA Plectin l Iso. 6 human (NP ) (2064.) ILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLA Plectin I Iso. 10 human (NP958785) (1931) IEALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLA

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15 Patent Application Publication Mar. 27, 2008 Sheet 14 of 27 US 2008/ A1 Desmoplakin human (NP ) Unnamed Mus cusculus (NP ) Plectin IBo. 6 Mus musculus (NP ) Sita. Plectin human (AAHO7597) Plectin 6 Rattus norvegicus (AAR95660) Pectin l human (Cl549) 5 human Plectin so. {NP ) Plectin I Iso. 10 human (NP ) Desmoplakin human (NP ) Onnamed Mus musculus (NP ) Plectin l iso. 6 Mus musculus (NP 95879) Sin. Plectin I human (AAHO7s57) Plectin 6 Rattus norvegicus (AAR95660) Plectin l human (Cl5149) Plectin l Iso. 6 human (NP958782) Plectin I Iso. 10 human (NP ) Desmoplakin human (NP ) Unnamed Mus musculus (NP ) Plectin l Iso. 6 Mus musculus (NP958791) Sin. Plectin I human (AAHO7597) Plectin 6 Rattus norvegicus (AARS 5660) Plectin l human (Qlsl49) Piectin l Iso. 6 human (NP ) Plectin I Iso. 10 human (NPL958785) Destroplakin human (NPOO4406) Unnamed Mus musculus (NP ) Plectin l Iso. 6 Mus musculus (NP ) Sim. Plectin. I human (AAHO7597) Plectin 6 Rattus norvegicus (AAR95660) Plectin l human (Q1549) Plectin l Iso. 6 human (NP ) Plectin I Iso. 10 human (NP ) Desmoplakin human (NP_ ) Unnamed Mus musculus (NP ) Plectin l Iso. 6 Mus musculus (NP958791) Sira. Plectin I human (AAHO7597) Plectin 6 Rattus norvegicus (AAR95660) Plectin i human (Q.5l 49) Plectin l Iso. 6 human (NP ) Plectin I Iso. 10 human (NP ) Desmoplakin human (NP_00440s) Unnamed Mus musculus (NP ) Plectin l Iso. 6 Mus musculus (NP958791) Sitn. Plectin I human (AAHO7597) Plectin 6 Rattus norvegicus (AAR95660) Plectin human (Qlsi49) Plectin 1 Iso. 6 human (NP958782) Plectin I Iso. 10 human (NP ) 1889) (l) (277) (l) (278) (274) (274) (258) l935) () (2766) (l) (2768) (2764) (2764) (263) (lig3s) (l) (2816) (l) (288) (284) (28l4) (2681) (193s) (l) (2866) (1) (2B68) (2864) (2864) (273) (193s) (l) (296) (l) (298) (29.14) (2914) (278) (l935) (l) (2966) (l) (2968) (2964) (2964) (283) OO erekns----lrseerlcaekrieercrrkledstretcsoletersr EOORQQQEKLAEENQRLRERLQRIEEEHRAALAHSEEASQAAATKA EggRRQQEELAEENQRLREQLQILEEcHRAALAHSEEVTASOVAATKTL EORROQEELAEENQRLREQLOLEEOHRAALAHSEEWTASOVAATKTL EQQRRQQEELIAEENQRLREQLOLLEEQHRAALAHSEEVASQVAATK SO PNGRDALDGPSMEAEPEYFEGLRQKVPAQQQEAGISMEELQRLTQGH PNGRDALDGPAAEAEPEHSFDGLRRKVSAORCEAGILSAEELORLAGH PNGRDALOGPAAEAEPEHSFGLRRKWSAORLQEAGILSAEEQRAQGH PNGRDALDGPAAEAEPEHSFDGLRRKVSAQRLQEAGILSAEELQRLAQGH 28S 2900 TTWAELTQREDVHRYLKGGSSIAGLLLKPTNEKLSVYTALQRQLLSPGTA TTVDeLaRREDVRHYLoGRssacLLKATNEKTSWYAALROLLSPGTA TTWDEL ARREDVRHYLOGRSSAGLLLKATNEKLSWYAALOROLLSPGTA TTVDELARREDVRHYLoGRSSIAGLLLKATNEKLSWYAALORQLLSPGTA LILLEAQAASGFLLDPWRNRRLIWNEAVKEGVWGPELHHELLSAERAVTG EAOAASGFLOPWRNRRLTWNEAVKEGVWGPELHHKSAERAVTG LILLEAQAASGFLLDPWRNRRLTVNEAVKEGVWGPEEHHKLLSAERAVTG LILLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPELHHEOLLSAERAVTG 29S 3000 YKDPYTGEQISLFQAMKKDLIVROHGIRLLEAQIATGGIEDPVHSHRVPV YKDPYTGoos FOAMokcLIVREHCIRLEAQIATGGVIDPVHSHRVPV YKDPYTGQQISLFOAMQKGLIVREHGIRLLEAQIATGGVIDPWHSHRWPW YKDPYTGQQISLFQAMQKGLIVRRHGIRLLEAQIATGGVIDPVHSHRVPV SO DWAYORGYFDEEMNRVLADPSDDTKGFFDPNTHENLTYLoLLERCVEDPR DVAYRRGYFDeEMNRVLADPsbDTKGFFDPNTHENLTYLOLLERCVED PE DWAYRRGYFDEEMNRVLADPSDDTKGFFDPNTHENTYLOLLERCVEDPE DWAYRRGYFDEEMNRVLADPSDDTKGFFDPNTHENITYLQLLERCVEDPE

16 Patent Application Publication Mar. 27, 2008 Sheet 15 of 27 US 2008/ A1 Desinoplakin human (NP_ ) Unnamed Mus musculus (NP ) Plectin l Iso. 6 Mus musculus (NP ) Sin. Plectin human (AAHO7597) Plectin 6 Rattus norvegicus (AAR95660) Plectin l human (Qisids) Plectin l Iso. 5 human (NP958782) Plectin I Ise. O human (NP ) Desinoplakin human (NP_ ) Unnamed Mus musculus (NP Plectin i Iso. 6 Mus musculus (NP 95879) Sin. Pectin human (AAHO7597) Plectin 6 Rattus norvegicus (AAR9566O) Plectin l human (Qls49) Piect in l Iso. 6 human (NP ) Plect in I Iso. O human (NP ) Desmoplakin human (NP_ ) Unnamed Mus musculus (NP ) Plectin i Iso. 6 Mus musculus (NP ) Sin. Plectin I human (AAHO7597) Plectin 6 Rattus norvegicus (AAR95660) Plectin l human (Qlsl49) Plectia l iso. 6 human (NP ) Plectin I Iso. i0 human (NP ) Desmoplakin human (NP ) Unnamed Mus musculus (NP ) Plectin. Iso. 6 Mus musculus (NP ) Sitn. Plectin human (AAHO7597) Plectin 6 Rattus norvegicus (AAR95660) Plectin l human (Q549) Plectin l Iso. 6 human (NP958782) Plectin I Iso. O human (NPL ) Desmoplakin human (NPOO4406) Unnamed Mus musculus (NP ) Plectin l Iso. 6 Mus musculus (NP ) Sin. Plectin human (AAHO7597) Plectin 6 Rattus nor vegicus (AAR95660 Plectin l human (Qlsl49) Plectin l Iso. 6 human (NP ) Plectin I Iso. 10 human (NPL958785) Desmoplakin human (NP_ ) Unnamed Mus musculus (NP ) Plectin l Iso. 6 Mus musculus (NP95879l) Sira. Pectin I human (AAHO7597) Plectin 6 Rattus norvegicus (AAR95660) Pectin hitman (Qls49) Plectin l iso. 6 human (NP ) Plectin I Iso. lo human (NP ) (i) (306)...) (308) (304) (3014) (288) (193s) (l) 3066) () (3068) (3064.) 3064.) (293) (1935) () (36) () (38) (34) (3ll 4) (2981) 193s) (i) (366) () (368) (3 is 4) (364) (303) (1935) (1) (326) (...) (32.8) (324.) 324 ) (308) (93S) () (3266) (i) 3268) (3264) (3264) 33) TGRPTDKAAKGGELVYTOTEARDWFEKATVSAPFGKFOGKTWWE TGLCLLPLTDKAAKGGEVYTDSEARDVFEKATVSAPPGKFOGKTV WE TGLCLLPLTDKAAKGGRVYTDSEARDVFEKATVSAPFGRFQGKTVTIWE TGLCLLPLTDKAAKGGELVYTDSEARDWFEKATVSAPFGKFOGKTVFIWE IINSEYFTAERRDLLRCFRTGRITVEKIKIWITWEEHERKGolcFSG IINSEYFTAEQRRDLLRQFRTGRITVERIIKIIITVVEEQEQKGRLCFEG INSEYFTAErrol LRRTGRITWEKIIKIITV WEEEKGRLCFEG INSEYFTAEORRDLERQFRTGRITVEKIKIIITV WEECEQKGRLCFRG LRAIWPAAELDSGVISHEVYCOLORGERSVREVAEAEWROARGTSWI LRSVPAAELESRWDRELYCOLORGERSWRDVAEWTWRRARGANW LRSLVPAAELLESRVIDRELYOOLORGERSVRDVAEWDTVRRALRGANV LRSLVPAAE.I.ESRVIDRELYQQLORGERSVRDVAEVDTVRRALRGANVI 32Ol AGWLEEAGOKLSYEARRDLOPEWAWALLEAQAGTGHIDPATSARL AGVWLEEAGQKLSYNALKKDLLPSDMAVALLEAQAGTGHIIDPATsARL AGVWLEEAGQKSIYNALKKDLLPSDMAVALLEAQAGTGHIIDPATSARL AGVWLEEAGOKLSIYNALKKDLLPSDMAVALLEAQAGTGHIIDPATSARL 32S 3300 TVOEAVRAGLVGPEMHEKLLSAEKAVTGYRDPYSGQSVSLFQALKKGLIP TwbeavrAGIWGPEFHEKLISAEKAVTGYRDPYTGOSVSLFQALKKGLIP WDEAWRAGLVGPEFHEKLLSAEKAVTGYRDPYTGSVSFQALKKGLIP TVDEAwRAGLWGPEFHEKLLSAEKAVTGYRDPYTGQSWSLFALKKGLIP REQGLRLLDAQLSTGGIVDPSKSHRVPLDVAYARGYLDKETNRAETSPRD REGLRLLDAQISTGGIVDPSKSHRWPLDVACARGCLDEETSRALSEPRA REGIRLLDAQLSTGGIVDPSKSHRVPLDVACARGCLDEETSRALSAPRA RECGIRLLDAQISTGGIWoPSKSHRWPWACARGCDEETSRALSAPRA

17 Patent Application Publication Mar. 27, 2008 Sheet 16 of 27 US 2008/ A1 Figure 2- Desmoplakin-Protein-Alignment - 13 Desmoplakin human (NP_ ) (1935) Unnamed Mus (musculus (NP ) Plectin Iso. 6 Mus musculus (NP 95879) () (336) Sin. Plectin human (AAHO7597) (l) Plectin 6 Rattus norvegicus (AAR95660) (3318) DARVYLDPSTREPVTYSQLQQRCRSDOLTGLSLLPLSEKAVRARQEEVYS Plectin l human (Qlsl49) (33ld) DAKAYSDPSTGEPATYGELQQRCRPDQLTGLSLLPLSEKAARARQEEFYS Plectin i Iso. 6 human (NP958782) (3314) DAKAYSDPSTGEPATYGELQQRCRPDQLTGLSLLPLSEKAARARQEELYS Plectin I Iso. O human (NP958785) (381) DAKAYSDPSTGEPATYGEQQRCRPDQLTGLSLLPLSEKAARARQEELYS 3. GO 3GSO Desmoplakin human (NP_ ) (1935) Unnamed Mus musculus (NP780547) (l) Plectin l Iso. 6 Mus musculus (NP 95879)) (3366) Sion. Plectin human (AAHO7597) (l) Plectin 6 Rattus nor vegicus (AAR95660) (336B) ELQARETLEKAKVEVPvgGFKGRALTwWELISSEYFTEEQRQELLROFRT Plectin l human (Q549) (3364) ELQARETFEKTPvEVPVGGFKGRTVTVWELISSEYFTAEQRQELFRQFRT Plectin l Iso. 6 human (NP ) Plectin I Iso. O human (NP958785) (3364) ELQARETFEKTPVEVPVGGFKGRTVTVWELISSEYFTAEQRQELLRQFRT (323i) ELQARETFEKTPvEvPvGGFKGRTvrvw ELISSEYFTAEORQELLRQFRT Desmoplakin human (NP ) (1935) YoREIDKIRQ Unnamed Mus musculus (NP ) () Plectin Iso. 6 Mus musculus (NP ) (3416) GKVTVEKWIKIWITIVEEVETRRQERLSFSGLRAPvPASELLDAKILSRA Sita. Plectin I human (AAHO7597) (l) r Plectin 6 Rattus norvegicus (AAR95660) Plectin human (Qlsl49) (3418) GKVTVEKVIKILITIVEEVETQRQERLSFSGLRAPvPASELLASKILSRT (344) GKVTVEKVIKILITIVEEVETLRQERLsPSGLRSPvPASELLAsgwlSRA Plectin l Iso. 6 human (NP ) Plectin I I so. 10 human (NP ) (3414) GKVTVEKVIKILITIVEEVETLRQERLSFSGLRAPvPASELLASGVLSRA (3281) GKVTVEKVIKILITIVEEvETLROERLSFSGLRAPvPASELLASGVLSRA Desmoplakin human (NP_ ) (1945) R a ar a r a or as us Unnamed Mus musculus (NP780547) (l) Plectin l Iso. 6 Mus musculus (NP95879l) (3466) QFDQLKDGKTSVKELSEVGSVRTLLQGSGCLAGIYLEDSKEKVTIYEAMR Sin. Plectin human (AAHO7597) (l) Plectin 6 Rattus norvegicus (AARs5660) (34.68) QFEQLKDGKTSWKDLSEVGSVRTLLQGSGCLAGIYLEDSKEKVTIYEAMR Plectia human (Qls49) (3464) QFEQLKDGKTTVKDLSELGSWRFLLQGSGCLAGIYLEDTKEKVSIYEAMR Piectin l Iso. 6 human (NP958782) 3464) QFEOLKDGKTTVKDLSELGSWRTLLQGSGCLAGIYLEDTKEKVSIYEAMR Plectin I Iso. 10 human (NP ) (3331) QFEQLKDGKTTvKDLSELGSVRTLLQGSGCLAGIYLEDTKEKVSIYEAMR Desmoplakin human (NP_ ) (1946) Unnamed Mus musculus (NP ) (1) Plectin l Iso. 6 Mus musculus (NP ) 3516) RGLLRPSTATLLLEAAATGFLVDPVRNQRLYWHEAVKAGVvGPELHEKL Sin. Plectin I human (AAHO7597) (l) r Plectin 6 Rattus norvegicus (AAR95660) (3518) RGLLRPSTATLLLEAQAATGFLVDPVRNQRLYWHEAVKAGVvGPELHEKL Pectin human (Q1549) (354) RGLRATIAALLLEAQAGTGFLWDPWRNQRLYWHEAVKAGVWGPELHEQL Plectin Iso. 6 human (NP958782) (3514) RGLLRATTAALLLEAQAATGFLVDPVRNQRLYVHEAVKAGVvGPELHEQL Plectin I so. O human (NP ) (338) RGLLRATTAALLLEAQAATGFLVDPWRNORLYWHEAVKAGVVGPELHEO Desmoplakin human (NPOO4406) (1946) Unnamed Mus musculus (NP780547) (l) Plectin l Iso. 6 Mus musculus (NP ) (3566) Sim. Plectin I human (AAHO7597) (l) Plectin 6 Rattus norvegicus (AAR95660) (3568) LSAEKAVTGYKDPYSGSTISLFQAMKKGLVLRDHAIRLLRAQIATGGIID Plectin l human (Qlsl49) (3564) LSAEKAVTGYRDPYSGRTISIFQAMKKGVLREHGIRLLEAQIATGGIID Plectin i Iso. 6 human (NP ) (3564) LSAEKAVTGYRDPYSGSTISLFQAMQKGLVLRQHGIRLLEAQIATGGIID Plectin I so. O human (NP ) (343) LSAEKAVTGYRDPYSGSTISLFQAMQKGVLRQHGIRLLEAQATGGEID

18 Patent Application Publication Mar. 27, 2008 Sheet 17 of 27 US 2008/ A1 Destroplakin human (NP ) Unnamed Mus musculus (NP ) Plectin l Iso. 6 Mus musculus (NP ) Sita. Pectin I human (AAHO7597) Plectin 6 Rattus corvegicus (AAR95560) Plectin human (Q.549) Plectin Iso. 6 human (NP958782) Plectin I Iso. O human (NP ) Desmoplakin human (NP_ ) Unnamed Mus musculus (NP ) Plectin l Iso. 6 Mus musculus (NP ) Sin. Plectin I human (AAHO7597) Plectin 6 Rattus norvegicus (AAR95660) Plectin human (Qls49) Plectin l Iso. 6 human (NP ) Plectin i Iso. 10 human (NP ) Desmoplakin human (NPOO4406) Unnamed Mus tausculus (NP ) Plectin l Iso. 6 Mus musculus (NP ) Sin. Plectin I human (AAHO7597) Plectin 6 Rattus norvegicus (AAR95660) Plectin l human (O549) Plectin l Iso. 6 human (NP ) Plectin I iso. 10 human (NP958785) Desinoplakin human (NP_ ) Unnamed Mus musculus (NP780547) Plectin l iso. 6 Mus musculus (NP ) Sin. Plectin I human (AAHO7597) Plectin 6 Rattus norvegicus (AAR95660) Plectin l human (OlSl49) Plectin Iso. 6 human (NP ) Plectin I Iso. 10 human (NP ) Desmoplakin human (NP_ ) Unnamed Mus musculus (NP ) Plectin l Iso. 6 Mus musculus (NP ) sin. Plectin I human (AAHO7597) Piect in 6 Rattus norvegicus (AAR95660) Plectin l human (Q549) Plectin i Iso. 6 human (NP ) Plectin I Iso. lo human (NPS58785) Desmoplakin human (NP_ ) Unnamed Mus musculus (NP780s47) Plectin l Iso. 6 Mus musculus (NP ) Sin. Plectin. I human (AAHO7597) Plectin 6 Rattus norvegicus (AARs566O) Plectin l human (Ql 549) Plectin i Igo. 6 human (NP9587 B2) Plectin I Ibo. 10 human (NP ) 946) () 35ls) (l) (368) (354) (3S4) 348) (1946) l) (3666) (9) (3668) 3664) (3664) 3531) 948) (l) (37l6) (59) (378) 374) (3714) (3581) ls 71.) (l) (3766) (los) (3768) (3764) (3764) 363) (2005) (l) 386) (59) 38l 8) (384) (384) (368) (2052) (l) (3866) (209) (386B) (3864) (3864) 373) PVHSHRLPWDVAYQRGYFDEEMNRVLADPSDDEKGFFDPNTHENLFYIQi ENLYRQL PWHSHRLPWDWAYoRGYFDEEMNRVLADPsootkesfront-ENEL PvNSHRWPVDVAYQRGYFSEEMNRVLADPSDDTKGFFDPNTHENLTYRQL. PVHSHRWPWDWAYORGYFSEEMNRVLADPsbOTKGFFPNTHENTYROL PVHSRWPVDWAYQRGYPSEEMENRVLADPsdor.cgfroPNTHENTYROL SO us as a a un n w us as us as an up PY LERCVED PETGLRLLPLKGAEKTEVVETTQVYTEEETRRAFEETOIDIPG LERCVEDPETGLRLLPLKGAEKAEVVETTQVYTEEETRRAFEETQIDIPG LERCVEDPETGLRLLPLRGAEKTEVVETTOWYTEEETRRAFEETOIDIPG LERCVEDPETGLRLLPLKGAEKVEVVETTQVYTEEETRRAFEETQIDIPG LERCVED PETGLRLLPLKGAEKAEVVETTOWYTEEETRRAFEETQIDIPG LERCVED PETGLRLEPLKGAEKAEvVETTQVYTEEETRRAFEETOIDIPG GSHRETOTECEWTVDTSKLVFDG GGSHGGSSMSLWEWMSNMIPEDORARLMADFOAGRVTKERMIII.E.I. GGSHGGSTMSWEVMQSDLIPEEQRACLMADFQAGRVTKERM IIIEII GGSHGGSSMSWEWMOSDMIPEDORARLMADFOAGRVTKERM IIIEII GGSHGGSTMSWEWMSDLIPEEQRALMADFQAGRWTKERM IIIEII GGSHGGSTMSLWEWMCSDLIPEEORACLMADFQAGRWTKERMIIIEII GGSHGGSTMSWEVMQSDLIPEEQRAQLMADFOAGRVTKERMIIIIIEI LRKKVTAMQLYECoLIDKTTLDKLLKGKKsweev EKTEIIRQQNLASYDYVRRRLTAEDLYEARIISLETYNLFREGTKNEREW EKTEIIROQGLASYDYVRRRLTASDLFEARIISIETYNLLREGTRSLREA EKTEIIRQQNLASYDYVRRRLTAEDLYEARISLETYNLFREGTKSLREW EKTEIRQOGASYDYVRRRLTGEDLFEARIISLETYNLLREGTKSLREA EKTEIIRQOGLASYOYVRRRLTAEDIFEARISLETYNLLREGTRSLREA EKTEEIRQQGLASYDYVRRRLTAEDLFEARIISLETYNLLREGTRSLREA AS--EQPFLRGAGSIAGASAS-PKEKYSLVEAKRKKLISPESTVMLLEA LEMESAWRYLYGGAVAGWYLPGSRQTLTIYALKKGLISAEVARLLLEA LEAESAWCYLYGTGSWAGWYLPGSROTESYQALKKGLSAEWARILLEA LEMESAWRYLYGTGSVAGVYLPGSRQTLTIYOALKKGLISAEVARLLEA EEGESAWFYLYGTGSWAGWYLPGSRTLSYQAKKGSAEVARLLEA LEAESAWCYLYGTGSWAGWYLPGSRQTLSYQALKKGLLSAEWARLLEA IEAESAWCYLYGTGSWAGWYLPGSRQTLSYQALKKGLESAEVARILLEA OAATGGDPHRNEKTWOSAIARDLIDFDDRQQIYAAEKAITGFDDPFS OAATGFLDPWKGERTWDEAVRKGLWGPEHRLLSAERAVTGYRDPYT QAATGFLOPVKGERLTWDEAWRKGLWGPELHORLESAERAWTGYRDPYT QAATGFLOPVKGERTVDEAVRKGLVGPELHDRLLSAERAWTGYRDPYT QAATGFLOPVKGERLTWDEAVRKGLVGPELDRLLSAERAWTGYRDPYT OAAGFLLDPWKGERWDEAWRKGWGPEHDRSAERAWGYROPY QAATGFLLDPVKGERLTVDEAVRKGLVGPELHDRLLSAERAVTGYRDPYT

19

20 Patent Application Publication Mar. 27, 2008 Sheet 19 of 27 US 2008/ A1 Figure Desmoplakin-Protein-Alignment Desmoplakin human (NPoD44 os) (24 Ol) LSEILSDPSDDTKGFFDPNTEENTYLOLKERCIKDEETGLCLLPLKEKK Unnamed Mus musculus (NP780547) (2) LSELSDPSTKGFFDPNTEENLYOKERCIKEETGCEPLKEKK Plectin l iso. 6 Mus trusculus (NPsss 79) (4215) MNEILTDPSDDTKGFFDPNTEENLFYIQMERCITDPQTGLCE-LPLKEKK Sita. Pectin i human (AAHOS97) (558) MNEELTPSDDTKGFFDPNTEENTYLERCITPorscLPLKEKK Plectin 6 Rattus norvegicus (AAR95660) (627) MNEILTDPSDDTKGFFDPNTEENLFYIQLMSRCITDPQTGLCLLPLKEKK Pectin human (O549) (423) MNEs.TDPsooksPDPNTEENLEYOLMERCITOPTGLCL,PIKEKK Plectin Iso. 5 human (NP ) (4213) MNEILTDPSDDTKGFFDPNTEENLTYLQLMERCITDPQTGLCLLPLKEKK Plectin I Iso. O human (NP ) (4080) M.NEILTOPSDDTKGFFDPNTEENLTYLQLMERCITDPOTGLCLLPLKEKK Desmoplakin human NP_ ) (245) Kovorso KNTLRKRRVVIVDPETNKEMSvoEAYKKGLIDYETFKELCEOE Unrathed Mus causculus (NP ) (62) KQWQTSQKNTLRKRRV-VIVDQETNKEMSVSAYKKGLIDYDTFKBLCEOE Plectin l Iso. 6 Mus musculus (NP ) (4265) RERKTsSKSSVRKRRVVIvpPETGKEMSVYEAYRKGLIDHQTYLELSEOE Sin. Plectin I human (AAHO7597) (608) RERKTSSKSSVRKRRVVIVPPETGKEMSVYEAYRKGLIDHQTYLRLSROR Plectin S Rattus norvegicus (AAR95660) (4.267). RRRKTSSKSSVRKRRVVIVDPETGKEMSVYEAYRKGLIDHOTYLELSEGE Plectin human (Qlsl49) (4263) RERKTSSKSSWRKRRVVIVDPETGKEMSVYRAYRKGLIDHOTYLELSEOR Plectin l Iso. 6 human (NP958782) (4263) RERKTsSKSSWRKRRVWIWPETGKEMSWYRAYRKGLIDHCTYLESECE Plectin I Iso. O human (NP ) (430) RERKTSSKSSVRKRRV VIVDPErgkEMSVYRAYRKGLIDHOTYLELSEQE Desmoplakin human (NP_ ) (25 Ol) CEWEEITTGSDGSTRWVLVDRKTGSQYDIQDAIDKGLVERKFFDQYRSG Unnamed Mus musculus (NP ) (112) CEWEEITITGSDGSTRVVLVDRKTGSQYDIQDAIDKGLWDRKFFDOYRSG Plectin l Iso. 6 Mus musculus (NP ) (4315) CEWEEITISSSDGVVKSMIIDRRSGRQYDIDDAITKNLIDRSALDQYRAG Sita. Plectia human (AAHO7597) 658) CEWEEITISSSocWWKSMIDRRSGRCYDDDAIAKNLIDRSADOYRAG Plectin 6 Rattus norvegicus (AAR95660) (437) CEWEEITISSSDGVVKSMIIDRRSGRQYDIDDAITKNLIDRSADQYRAG Plectin humaia (Q549) (433) CEWEEITISSSDGVWKSMIDRRSGROYDDDAIAKNLIDRSADCYRAG Plectin l Iso. 6 human (NP ) (433) CENEEITISSSDGVVKSMIIDRRSGRQYDIDDAIAKNLIDRSADCYRAG Plectin I iso. 10 human (NP ) (480) CEWEEITISSSDGWWKSMDRRSGRQYDEDDAIAKNLIORSADCYRAG Desmoplakin human (NP ) (2551) SLSLTQFADMISLKNGVGTSSSMGSGVSDDVFSSSRHESVSKISTISSVR Unnamed Mus musculus (NP ) (62) SSLTCFADMISLKNGVGNSSGGGSVNDDVFSSSRHDSWSKSTISSVR Plectin IBO. 6 Mus musculus (NP ) (4365) TLSITEFADMLSGNAGGFRSR SSSWGSSS SYSSA Sin. Pectin I human (AAHO7597) (708) TLSITEFAOMSGNAGGFRSR SSSWGSSS SYPISA Plectin 6 Rattus norvegicus (AARs 5660) (4367) TLSITEFADMLSGNAGGFRSR SSSWGSSS SYPSSA Plectin human (Qlsl49) 4363) TLSITEFADMSGNAGFRSR SSSWGSSS SYPISPA Plectin l Iso. 6 human (NP ) (43.63) TSITEFACMSGNAGGFRSR SSSWGSSS SPSA Plectin I Iso. 10 human (NP ) (4230) TLSITEFADMLSGNAGGFRSR SSSWGSSS SYPISPA Desmoplakin human (NPOD44.06) (26 Ol) NLTIRSSSFSDTLEESSPIAAIFDTENLEKISITEGIERGIVDSITGQRL Unnamed Mus musculus (NP ) (212). NTRSSSLSDPIEESSPIAAIFTENLEKISIAEGIERGWDSITGORL Plectin Iso. 6 Mus musculus (NPs58791) (44 Ol). GPRTOLASWSDPTEETGPWAGILDTETLEKVSITEAMHRNLVDNITGQRL sin. Plectin I human (AAHO7597) (744) WSRTOLASWSDPTEETGPWAGILDTETLEKVSITEAMHRNLVDNITGQRL Plectin 6 Rattus norvegicus (AAR95660) (4403) VPRTQLASWSDPTEETGPVAGILDTETLEKVSITEAMHRNLVDNITGQRL Plectin l human (Q.5l 49) (4.399) WSRTQLASWSEPTEETGPWAGILDTETLEKVSITEAMHRNLVDNITGQRL Plectin l Iso. 6 human (NP ) (4399) VSRTOLASWSDPTSETGPWAGILDTETLEKVSITEAMHRNLVDNITGQRL Plectin I Iso, l0 human (NP ) (4.266) WSRTQLASWSDPTEETGPWAGILDTETLEKVSITEAMHRNLVDNITGQRL SO Destinoplakin human {NP_ ) (265l) LEAQACTGGIIHPTTGQKLSLQDAVSQGVIDODMATSVKPAQKAFIGFEG Unnamed Mus musculus (NP ) (262) LEAQACTGGIIHPTTGQKLSLQDAVNOGLIDQDMATRIKPAOKAFIGFEG Plectin l Iso. 6 Mus musculus (NP ) (445l) LEAQACTGGIIDPSTGERFPVTEAVNKGLVDKIMVDRINAOKAFCGFED Sin. Plectila I human (AAHO7597) (794) LEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMVDRINLAQKAFCGFED Plectin 6 Rattus norvegicus (AAR95660) (4453) LEAQACTGGIIDPSTGERFPvTEAVNKGLVDKIMVDRINAQKAFCGFED Plectin l human (Q.5l 49) (4449) LEAQACTGGIIDPSTGERLPVTDAVNKGLVDKIMVDRINLAQKAFCGFED Plectin l Iso. 6 human (NP958782) (4449) LEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMVDRINLAQKAFCGFED Plectin I iso. 10 human (NPL958785) (43 les) LEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMVPRINLAQKAFCGFED

21 Patent Application Publication Mar. 27, 2008 Sheet 20 of 27 US 2008/ A1 Figure 2 - Desmoplakin-Protei Alignmen 45S 4500 Desmoplakin human (NP ) 270) WKGKKKMSAAEAVKEKWLPYEAGQRFLEFQYTGGLVDPEVHGRISTERA Unnamed Mus musculus (NP ) (32) WKGKKKMsAAAVKEKWIPYEAGORFLEFOFLIGGLVDPEVHGRISTEEA Plectin i Iso. 6 Mus musculus (NP ) (45 Ol) PRTKTKMSAAQALKKGWLYYEAGQRFLEVOYLIGGLIEPDTPGRWSIDEA Sin. Plectin human (AAHO7597) (844) PRTKTKMSAAQALKKGWLYYEAGORFLEVOYLEGGLIEPOTPGRVPLOEA Plectin 6 Rattus norvegicus (AAR9566O) (4503) PRTKKMSAAQALKKGWLYYEAGORFLEVOYLTGGLIEPDTPGRVSLDEA Plectin l human (Q.5l 49) (4499) PRTKTKMSAAQALKKGWLYYEAGORFLEVOYLTGGLIEPDTPGRVPLDEA Plectin Iso. 5 human (NP ) (4499) PRTKTKMSAAQALKKGWLYYEAGQRFLEvoyLigGLIEPDTPGRVPLDEA Plectin I Iso. 10 human (NP958785) (4.366) PRTKTKMSAAQAIKKGWIYYEAGORFLEWQYGGLEPFPGRVPLEA SO Desmoplakin human (NPoo4406) (2751) IRKGFIDGRAAQRLQDTSSYAKILTCPKTKLKISYKDAINRsMVEDITGL unnamed Mus musculus (NP ) (362) IRKGFIDGRAAORQDISSYAKITCPKTKLKSYKDAMNRsMVEDTG Plectin l Iso. 6 Mus musculus (NP ) (4551) LQRGTVDARTAQKLRDVSAYSKYLTCPKTKLKISYKDALDRSMVEEGTGL Sin. Plectin human (AAHO7597) (894) LORGTVARTAOKLRDWGAYSKYLTCPCTKLKSYKDALRsMVEEGTG. Plectin 6 Rattus norvegicus (AAR9566O) (4553) LQRGTVDARTAQ:KLRDVSAYSKYLTCPKTKLKISYKDALDRSMVEEGTGL Plectia human (Cls.49) (4549) LORGTVDARTAQKLRDWGAYSKYLTCPKTKLKISYKDALDRSMVEEGTGL Plectin l Iso. 6 human (NP ) (4549) LORGTVdARTAQKLRDVGAYSKYiTCPKTKLKISYKDALDRSMVREGTGL Piectin I Iso. lo hunan (NP ) (44.16) LRGTVDARAQKRDWGAYSKYLTCPKTKLKISYKDALDRSMWEEGTG. 45S 4700 Desmoplakin human (NP_ ) (2801) RLLEAASWSSKGPSPYNMSSAPGSRSGSRSGSRSGSRSSRSGSRRGSF Unnamed Mus musculus (NP ) (412) RLLEAASVSSKGLPSPYNMSAT-GSRSGSRSGSRSGSRSGSRSGSRRGSF Plectin i Iso. 6 Mus musculus (NP 95879i) (460i) RLLEAAAQSSKGYYSPYSVSGs----- GSTAGSRTGSRTGSRAGSRRGSF Sin. Plectin human (AAHO7597) (944) REAAAOSKYYSPYSWSGS GSTAGSRGSRTGSRAGSRRGSF Plectin 6 Rattus norvegicus (AAR9566O) (4603) RLLEAAAoSSKGYYSPYSVSGS GSTAGSRGSRTGSRAGSRRGSF Plectin l human (Q549) (4599) RLLEAAAQSTKGYYSPYSWSGS GSAGSRGSRTGSRACSR.RCSF Plectin i Iso. 6 human (NP s58782) Plectin I Iso. 10 human (NP ) (4599) RLLEAAAQSTKGYYSPYSVSGS GSTAGSRTGSRTGSRAGSRRGSF (4.466) RLLEAAAQSTKGYYSPYSVSGS GSTAGSRTGSRTSRAGSRRGSF l Desmoplakin human (NP ) (2851) DATGNSSYSYSYSFSSSSIGH Unnamed Mus musculus (NP ) (461) DATGNSSYSYSYSFSSSSIGGY Plectin l Iso. 6 Mus musculus (NP ) (4646) DATGSGFSMTFSSSSYSSSGYGRRYASGPSASLGGPESAVA Sim. Plectin. I human (AAHO7597) 989) datgscfsmtfssssysssgygrryasgssaslggpesawa Plectin 6 Rattus norvegicus (AAR95660) (.4648) DATGSGFSMTFSSSSYSSSGYGRRYASGPSASLGGPESAVA Plectin a human (Q1549) (46.44) DATGSGFSMTFSSSSYSSSGYGRRYASGSSASLGGPESAVA Plectin Iso. 6 human (NP ) (46.44 datgsgfsmtfssssysssgygrryasgssaslggpesava Plectin I. Iso. 10 human (NPs 58785) (45.) DATGSGFSMTFSSSSYSSSGYGRRYASGSSASLGGPESAVA

22 Patent Application Publication Mar. 27, 2008 Sheet 21 of 27 US 2008/ A1 T5 Transcription Start T5 Promoter --Fi. initation ATG 6x His-Tag coding Sequence SacI (62) Beta-LactamaSe poe30-kbd-b 4321 bp CoE OR Termination Region Figure 3: Vector map of poe30-kbd-b for expressing keratin-binding domain B

23 Patent Application Publication Mar. 27, 2008 Sheet 22 of 27 US 2008/ A1 5'AOX1-Promoter Clai (7666) Apa LI (731O) PstI (6888) N. Initiation ATG EcoRI (9) Ban HI (8678) HindIII (273) A. HindIII (8362) (8612) Ban.H. ann H. (368 (3 ) KBD-B s 6x His-tag coding sequence PES (923Stop EcoRI (939) 3'AOX (termination region) HindIII (1298) Clai (1305) plib15 HindIII (1310) 8681 bp Apa LI - Apa LI (5566) N HS4 3' AOX1-Fragment Nicol (3349) Figure 4: Vector map of plib15 for expressing the keratin-binding domain B

24 Patent Application Publication Mar. 27, 2008 Sheet 23 of 27 US 2008/ A1 Clai (ill) 5'AOX1-Promoter Apal (8702) Apal (807) HindIII (no57) Pst (828O) Ban HI (123) initation ATG Pst (1160) indiii (1665) BamHI (1760) Nicol (4741) ClaI (2697) HIS4 Pst (2311) HindIII (2315) stop EcoRI (2331) HindIII (2690) HindIII (27O2) 3'AOX (termination region) Figure 5: Vector map of plib16 for expressing the keratin-binding domain B

25 Patent Application Publication Mar. 27, 2008 Sheet 24 of 27 US 2008/ A1 atts ATG 6x His -tag coding sequence Aval (5495) Bay. PSE483) Clal (5481) Hin atts2 HindIII (5474) EcoRI (5462 BamHI (5449) Aua I (515O) alca EcoRI (4736) Pst (4734) Sna C AvaI(4724) N S \N, as W plib bp Xnd 0.7 Bann HI (47.85 sapal (2027) HindIII (469O) 4. Ncol (4OOO) argb / HindIII (36385 Figure 6: Vector map of plib19 for expressing the keratin-binding domain B

26 Patent Application Publication Mar. 27, 2008 Sheet 25 of 27 US 2008/ A1 Substrate (TMB) ColorleSS Product yellow Keratin-binding domain Figure 7: Quantitative KBD activity test: a His tag antibody-peroxidase conjugate is coupled via the His tag to skin- or hair-bound KBD. The peroxidase catalyzes a color reaction, the endpoint of which has a yellow Color which can be determined photometrically.

27 Patent Application Publication Mar. 27, 2008 Sheet 26 of 27 US 2008/ A1 Keratin binding domain Keratin N- - Na" (CH-NH O 5 O (Alexa Fluor 532) O o O -SS KBD-SH Dry - Dye1N KBO O O Figure 8: Coupling of the dye Alexa Fluor 532 to a cysteine thiol group of KBD-B.

28 Patent Application Publication Mar. 27, 2008 Sheet 27 of 27 US 2008/ A1 Figure 9: a) KBD-B-Alexa Fluor 532 coupling to human hair. Fluorescence micrograph (detection with absorption: 532 nmlemission: 590 nm). b)comparative Control with hair plus Alexa Fluor: 532 (without Coupled KBD-B).

29 US 2008/ A1 Mar. 27, 2008 KERATIN-BINDING POLYPEPTIDES PRIOR ART 0001 Vertebrate cells comprise filaments, one group of which is composed of keratins. These keratins also occur in hair, skin and nails, and specific proteins such as, for example, desmoplakin bind thereto by means of a special sequence motif called a keratin-binding domain (Fontao L. Favre B, Riou S, Geerts D, Jaunin F. Saurat J H, Green KJ, Sonnenberg A, Borradori L., Interaction of the bullous pemphigoid antigen 1 (BP230) and desmoplakin with inter mediate filaments is mediated by distinct sequences within their COOH terminus., Mol Biol Cell May: 14(5): Epub 2003 Jan. 26: Hopkinson SB, Jones J.C., The N terminus of the transmembrane protein BP180 interacts with the N-terminal domain of BP230, thereby mediating keratin cytoskeleton anchorage to the cell Surface at the site of the hemidesmosome, Mol Biol Cell January; 11(1): ). OBJECT OF THE INVENTION It is an object of the present invention to provide novel polypeptides which have a high affinity for keratin or keratin-containing materials such as skin or hair. Such polypeptides are Suitable for the cosmetic and pharmaceu tical treatment of keratin-containing structures, in particular of hair and skin. DESCRIPTION OF THE INVENTION The invention relates to cosmetic compositions for treating keratin-containing materials, comprising at least one keratin-binding polypeptide sequence (i) in a cosmetically compatible medium. Polypeptide Sequences (i) The polypeptide sequence (i) has a binding affinity for a keratin. The binding of polypeptide sequence (i) to a keratin can be assayed under the conditions described in examples 8, 9 and Particularly suitable keratin-binding polypeptides are the sequences which are present in human desmoplakin or are derived therefrom by modification of the human desmoplakin polypeptide sequences such as amino acid insertions, Substitutions or deletions The polypeptide sequence of human desmoplakin is depicted in SEQ ID No: 1. A suitable keratin-binding domain (domain B) is the polypeptide sequence SEQID No: 1 position 2193 to 2481, and the functional equivalents thereof. A further keratin-binding domain (domain C) is the polypeptide sequence SEQID No. 1 position 2606 to 2871, and the functional equivalents thereof The keratin-binding domains are depicted in FIG Preferred polypeptide sequences (i) include an amino acid sequence as shown in SEQ ID No: Also included according to the invention are like wise functional equivalents of the specifically disclosed polypeptide sequences (i) and the use thereof in the methods of the invention Functional equivalents' or analogs of the specifi cally disclosed polypeptides (i) are for the purposes of the present invention polypeptides which differ therefrom and which additionally have the desired biological activity such as, for example, keratin binding. Thus, for example, func tional equivalents' mean polypeptide sequences which show in one of the binding assays described in example 9 or 10 a binding of at least 10%, preferably at least 50%, particularly preferably 75%, very particularly preferably 90%, of the binding shown by a polypeptide having domain B or domain C of SEQ ID No. 1 in the binding assay described in example 9 or Examples of suitable amino acid substitutions are to be found in the following table: Original residue Ala Arg ASn Asp Cys Gln Glu Gly His Ile Leu Lys Met Phe Ser Thr Trp Tyr Val Substitution examples Ser Lys Gln: His Glu Ser ASn Asp Pro ASn; Glin Leu; Val Ile: Val Arg: Gln; Glu Leu: Ile Met; Leu: Tyr Thr Ser Tyr Trp; Phe Ile: Leu It is known that the serine naturally occurring at position 2849 in SEQID No: 1 can be replaced for example by glycine in order to avoid phosphorylation at this position (Fontao L. Favre B, Riou S, Geerts D, Jaunin F. Saurat J H. Green KJ, Sonnenberg A, Borradori L., Interaction of the bullous pemphigoid antigen 1 (BP230) and desmoplakin with intermediate filaments is mediated by distinct sequences within their COOH terminus. Mol Biol Cell May: 14(5): Epub 2003 Jan. 26) Functional equivalents mean according to the invention in particular also muteins which have, in at least one sequence position of the abovementioned amino acid sequences, an amino acid other than that specifically men tioned, but nevertheless have one of the abovementioned biological activities. Functional equivalents' thus include the muteins obtainable by one or more amino acid additions, Substitutions, deletions and/or inversions, it being possible for said modifications to occur in any sequence position as long as they lead to a mutein having the property profile according to the invention Functional equivalents in the above sense are also precursors of the described polypeptides, and func tional derivatives and salts' of the polypeptides Precursors' are in this connection natural or syn thetic precursors of the polypeptides with or without the desired biological activity The term "salts' means both salts of carboxyl groups and acid addition salts of amino groups of the protein molecules of the invention. Salts of carboxyl groups can be prepared in a manner known per se and include inorganic salts such as, for example, Sodium, calcium, ammonium, iron and Zinc salts, and salts with organic bases such as, for example, amines, such as triethanolamine, arginine, lysine,

30 US 2008/ A1 Mar. 27, 2008 piperidine and the like. The invention likewise relates to acid addition salts such as, for example, salts with mineral acids such as hydrochloric acid or sulfuric acid and salts with organic acids such as acetic acid and oxalic acid Functional derivatives of polypeptides of the invention can likewise be prepared on functional amino acid side groups or on the N- or C-terminal end thereof by means of known techniques. Such derivatives include for example esters or thioesters of carboxylic acid groups, amides of carboxylic acid groups, obtainable by reaction with ammo nia or with a primary or secondary amine; N-acyl derivatives of free amino groups prepared by reaction with acylating agents: N-alkyl derivatives of free amino groups prepared by reaction with alkylating agents; S-acyl derivatives of free mercapto groups prepared by reaction with acylating agents; thioethers by reaction of free mercapto groups with alkylat ing agents; disulfides by reaction of free mercapto groups, for example with thiols; O-acyl derivatives of free hydroxy groups prepared by reaction with acylating agents; or ethers by reaction of free hydroxyl groups with alkylating agents Functional equivalents' naturally also include polypeptides which are obtainable from other organisms, and naturally occurring variants. It is possible for example to establish ranges of homologous sequence regions by comparison of sequences, and to ascertain equivalent enzymes based on the specific requirements of the invention Functional equivalents likewise include frag ments, preferably single domains or sequence motifs, of the polypeptides of the invention, which have, for example, the desired biological function Functional equivalents' are additionally fusion proteins which comprise one of the abovementioned polypeptide sequences or functional equivalents derived therefrom and at least one further, heterologous sequence which is functionally different therefrom and is in functional N- or C-terminal linkage (i.e. with negligible mutual func tional impairment of the parts of the fusion protein). Non limiting examples of Such heterologous sequences are, for example, signal peptides or enzymes Functional equivalents also included in the invention are homologs of the specifically disclosed pro teins. These have a homology of at least 50%, preferably at least 75%, in particular at least 85%, such as, for example, 90%. 95% or 99%, with one of the specifically disclosed amino acid sequences calculated by the algorithm of Pearson and Lipman, Proc. Natl. Acad, Sci. (USA) 85 (8), 1988, A percentage homology of a homologous polypeptide of the invention means in particular percentage identity of the amino acid residues based on the total length of one of the amino acid sequences specifically described herein In the case of possible protein glycosylation, func tional equivalents' of the invention include proteins of the type defined above in deglycosylated or glycosylated form, and modified forms obtainable by altering the glycosylation pattern In the case of possible protein phosphorylation, functional equivalents of the invention include proteins of the type defined above in dephosphorylated or phosphory lated form, and modified forms obtainable by altering the phosphorylation pattern Homologs of the polypeptides (i) of the invention can be generated by mutagenesis, e.g. by point mutation or truncation of the protein Homologs of the polypeptides of the invention can be identified by screening combinatorial libraries of mutants, such as, for example, truncation mutants. For example, a library of protein variants can be generated by combinatorial mutagenesis at the nucleic acid level. Such as, for example, by enzymatic ligation of a mixture of synthetic oligonucleotides. There is a large number of methods which can be used to prepare libraries of potential homologs from a degenerate oligonucleotide sequence Chemical synthesis of a degenerate gene sequence can be carried out in an automatic DNA synthesizer, and the synthetic gene can then be ligated into a Suitable expression vector. The use of a degenerate set of genes makes it possible to provide all the sequences which encode the desired set of potential protein sequences in one mixture Methods for synthesizing degenerate oligonucle otides are known to the skilled worker (e.g. Narang, S. A. (1983) Tetrahedron 39:3: Itakura et al. (1984) Annu. Rev. Biochem. 53:323: Itakura et al., (1984) Science 198: 1056; Ike et al. (1983) Nucleic Acids Res. 11:477) Several techniques are known in the art for screen ing gene products in combinatorial libraries which have been prepared by point mutations or truncation, and for screening cdna libraries for gene products having a selected property. These techniques can be adapted to the rapid screening of gene libraries which have been generated by combinatorial mutagenesis of homologs of the invention. The most commonly used techniques for Screening large gene libraries, which are subject to high-throughput analy sis, include the cloning of the gene library into replicable expression vectors, transformation of suitable cells with the resulting vector library and expression of the combinatorial genes under conditions under which detection of the desired activity facilitates isolation of the vector which encodes the gene whose product has been detected. Recursive ensemble mutagenesis (REM), a technique which increases the fre quency of functional mutants in the libraries, can be used in combination with the screening tests to identify homologs (Arkin and Yourvan (1992) PNAS 89: ; Delgrave et al. (1993) Protein Engineering 6(3): ) A particularly advantageous embodiment of the invention are polypeptide sequences (i) which include at least one of the following polypeptide sequences, 0030) a) the polypeptide sequence SEQ ID NO: 1 position 2193 to 248 (domain B) 0031 b) the polypeptide sequence SEQ ID NO: 1 position 2606 to 2871 (domain C) c) a polypeptide sequence which is modified compared with (a) in up to 60% of the amino acids, 0033 d) a polypeptide sequence which is modified compared with (b) in up to 50% of the amino acids, with the proviso that the keratin binding of polypeptide sequence (c) or (d) amounts to at least 10% of the value shown by polypeptide sequence (a) or (b), measured in the assay described in example 9 or 10. Domain B or C means in this connection the keratin-binding domains, described above, of human desmoplakins (SEQ ID No: 1). 0034) Modification of amino acids thereby means amino acid Substitutions, insertions and deletions or any combina tions of these three possibilities Polypeptide sequences (i) preferably used are those having a highly specific affinity for the desired organisms. Accordingly, for applications in skin cosmetics, the polypep tide sequences (i) preferably employed are those having a

31 US 2008/ A1 Mar. 27, 2008 particularly high affinity for the keratin of human skin. The polypeptide sequences preferred for applications in hair cosmetics are those having a particularly high affinity for the keratin of human hair For applications in the pet sector, correspondingly, besides the polypeptide sequences described (SEQ ID NO:1), the preferred polypeptide sequences (i) are those having a particularly high affinity for the corresponding keratin, for example canine keratin or feline keratin However, it is also possible to use more than one polypeptide sequence (i) in the effector molecule of the invention, for example a sequence (i) which has a high binding affinity for the keratin of human skin, in conjunction with a sequence (i) which has a high affinity for the keratin of human hair. It is also possible for a plurality of copies of the same polypeptide sequence (i) to be connected consecu tively in order, for example, to achieve higher binding Suitable keratin-binding polypeptide sequences (i) are known. For example, desmoplakins and plectins com prise keratin-binding domains. (Fontao L. Favre B. Riou S, Geerts D, Jaunin F. Saurat J. H. Green KJ, Sonnenberg A. Borradori L., Interaction of the bullous pemphigoid antigen 1 (BP230) and desmoplakin with intermediate filaments is mediated by distinct sequences within their COOH termi nus., Mol Biol Cell May: 14(5): Epub 2003 Jan. 26; Hopkinson S. B. Jones J C. The N terminus of the transmembrane protein BP180 interacts with the N-terminal domain of BP230, thereby mediating keratin cytoskeleton anchorage to the cell surface at the site of the hemidesmo some, Mol Biol Cell January; 11 (1):277-86) It is possible for such regions to be mapped and identified by alignments of Such known protein sequences, for example using a computer program Such as Vector NTI 8 (Version of 25 Sep. 2002) supplied by InforMax Inc Further suitable polypeptide sequences (i) with good binding to human keratin are sequence regions which show high homology or sequence identity in an alignment and can be regarded as consensus sequences of the keratin binding domains Particular preference is sequence regions to the following: given among these domain B (KBD-B): polypeptide sequence SEQ ID NO: 1 position 2193 to 2448 domain B (KBD-B): polypeptide sequence SEQ ID NO: 1 position 2209 to 2448 domain C (KBD-C): polypeptide sequence SEQ ID NO: 1 position 2606 to 2871 domain C (KBD-C): polypeptide sequence SEQ ID NO: 1 position 2616 to 2871 domain C (KBD-C): polypeptide sequence SEQ ID NO: 1 position 2616 to 2811 domain C (KBD-C): polypeptide sequence SEQ ID NO: 1 position 2606 to It is known that the serine naturally occurring at position 2849 in SEQID NO: 1 can be replaced for example by glycine in order to avoid phosphorylation at this position and thus to ensure binding of domain C at the corresponding keratin (Fontao L. Favre B. Riou S, Geerts D, Jaunin F, Saurat J. H. Green KJ, Sonnenberg A, Borradori L., Inter action of the bullous pemphigoid antigen 1 (BP230) and desmoplakin with intermediate filaments is mediated by distinct sequences within their COOH terminus. Mol Biol Cell May: 14(5): Epub 2003 Jan. 26) If it is desired that the polypeptide sequences (i) have particularly good binding to a keratin from a non human organism, the sequence motifs selected as Suitable will preferably be those from the keratin-binding protein, e.g. desmoplakin or plectin, of the appropriate organism FIG. 2 shows an alignment of keratin-binding molecules The keratin-binding polypeptides (i) according to the invention can also, if desired, easily be separated from the keratin again. For this purpose it is possible to employ for example washing with keratin, whereby the keratin binding polypeptides (i) are displaced from their existing binding to the keratin and are saturated with the keratin from the washing Solution. Alternatively, a washing with a high content of detergent (e.g. SDS) is also possible for the washing out The keratin-binding polypeptides (i) according to the invention have a wide area of application in human cosmetics, in particular in skin, nail and hair care, animal care, leather care and leather processing The keratin-binding polypeptides (i) according to the invention are preferably used for skin cosmetics. They permit a high concentration and long action time of skin care or skin-protecting effectors Suitable auxiliaries and additives for producing hair cosmetic, nail cosmetic or skin cosmetic preparations are known to the person skilled in the art and can be found in handbooks of cosmetics, for example Schrader, Grund lagen und ReZepturen der Kosmetika Fundamentals and formulations of cosmetics, Hüthig Verlag, Heidelberg, 1989, ISBN The cosmetic compositions according to the inven tion may be skin cosmetic, nail cosmetic, hair cosmetic, dermatological, hygiene or pharmaceutical compositions Preferably, the compositions according to the invention are in the form of a gel, foam, spray, ointment, cream, emulsion, Suspension, lotion, milk or paste. If desired, liposomes or microspheres can also be used The cosmetically or pharmaceutically active com positions according to the invention can additionally com prise cosmetically and/or dermatologically active ingredi ents and auxiliaries Preferably, the cosmetic compositions according to the invention comprise at least one keratin-binding polypep tide sequence (i) as defined above, and at least one constitu ent different therefrom which is chosen from cosmetically active ingredients, emulsifiers, Surfactants, preservatives, perfume oils, thickeners, hair polymers, hair and skin con ditioners, graft polymers, water-soluble or dispersible sili cone-containing polymers, photoprotective agents, bleaches, gel formers, care agents, colorants, tints, tanning agents, dyes, pigments, consistency regulators, moisturizers, re fatting agents, collagen, protein hydrolysates, lipids, anti oxidants, antifoams, antistats, emollients and softeners. The keratin-binding polypeptide active ingredients may also be present in encapsulated form in the cosmetic preparations Advantageously, the antioxidants are chosen from the group consisting of amino acids (e.g. glycine, histidine, tyrosine, tryptophan) and derivatives thereof, imidazoles (e.g. urocanic acid) and derivatives thereof, peptides Such as D.L-carnosine, D-carnosine, L-carnosine and derivatives thereof (e.g. anserine), carotenoids, carotenes (e.g. B-caro tene, lycopene) and derivatives thereof, chlorogenic acid and derivatives thereof, lipoic acid and derivatives thereof (e.g.

32 US 2008/ A1 Mar. 27, 2008 dihydrolipoic acid), aurothioglucose, propylthiouracil and other thiols (e.g. thioredoxin, glutathione, cysteine, cystine, cystamine and the glycosyl, N-acetyl, methyl, ethyl, propyl. amyl, butyl and lauryl, palmitoyl, oleyl, Y-linoleyl, choles teryl and glyceryl esters thereof) and salts thereof, dilauryl thiodipropionate, distearyl thiodipropionate, thiodipropionic acid and derivatives thereof (esters, ethers, peptides, lipids, nucleotides, nucleosides and salts), and Sulfoximine com pounds (e.g. buthionine Sulfoximines, homocysteine Sulfox imines, buthionine Sulfones, penta-, hexa-, heptathionine Sulfoximine) in very low tolerated doses (e.g. pmol to umol/kg), also (metal) chelating agents (e.g. C-hydroxy fatty acids, palmitic acid, phytic acid, lactoferrin), C-hydroxy acids (e.g. citric acid, lactic acid, malic acid), humic acid, bile acid, bile extracts, bilirubin, biliverdin, EDTA and derivatives thereof, unsaturated fatty acids and derivatives thereof (e.g. Y-linolenic acid, linoleic acid, oleic acid), folic acid and derivatives thereof, ubiquinone and ubiquinol and derivatives thereof, vitamin C and derivatives thereof (e.g. Sodium ascorbate, ascorbyl palmitate, Mg ascorbyl phos phate, ascorbyl acetate), tocopherol and derivatives (e.g. Vitamin E acetate, tocotrienol), Vitamin A and derivatives (vitamin A palmitate), and coniferyl benzoate of benzoin resin, rutinic acid and derivatives thereof, C.-glycosylrutin, ferulic acid, furfurylideneglucitol, carnosine, butylhydroxy toluene, butylhydroxyanisole, nordihydroguaiacic acid, nor dihydroguaiaretic acid, trihydroxybutyrophenone, uric acid and derivatives thereof, mannose and derivatives thereof, Zinc and derivatives thereof (e.g. ZnO, ZnSO), selenium and derivatives thereof (e.g. selenomethionine), stilbenes and derivatives thereof (e.g. stilbene oxide, trans-stilbene oxide) Customary thickeners in such formulations are crosslinked polyacrylic acids and derivatives thereof, polysaccharides and derivatives thereof. Such as Xanthan gum, agar-agar, alginates or tyloses, cellulose derivatives, e.g. carboxymethylcellulose or hydroxycarboxymethylcel lulose, fatty alcohols, monoglycerides and fatty acids, poly vinyl alcohol and polyvinylpyrrolidone. Preference is given to using nonionic thickeners Suitable cosmetically and/or dermatologically active ingredients are, for example, coloring active ingredi ents, skin and hair pigmentation agents, tinting agents, tanning agents, bleaches, keratin-hardening Substances, anti microbial active ingredients, photofilter active ingredients, repellent active ingredients, Substances with a hyperemic effect, substances with a keratolytic and keratoplastic effect, antidandruff active ingredient, antiphlogistics, Substances with a keratinizing effect, active ingredients with an anti oxidative or free-radical-scavenging effect, Substances which moisturize the skin or keep the skin moist, re-fatting active ingredients, antierythimatous or antiallergic active ingredients, branched fatty acids such as 18-methyl eicosanoic acid, and mixtures thereof Active ingredients which tan the skin artificially and which are suitable for tanning the skin without natural or artificial irradiation with UV rays are, for example, dihydroxyacetone, alloxan and walnut shell extract. Suitable keratin-hardening Substances are usually active ingredients as are also used in antiperspirants, such as, for example, potassium aluminum sulfate, aluminum hydroxychloride, aluminum lactate, etc Antimicrobial active ingredients are used to destroy microorganisms or to inhibit their growth and thus serve both as preservatives and also as deodorizing Sub stance which reduces the formation or the intensity of body odor. These include, for example, customary preservatives known to the person skilled in the art, such as p-hydroxy benzoic esters, imidazolidinylurea, formaldehyde, sorbic acid, benzoic acid, Salicylic acid, etc. Such deodorizing Substances are, for example, Zinc ricinoleate, triclosan, undecylenic alkylolamides, triethyl citrate, chlorhexidine etc Suitable preservatives to be used advantageously according to the invention are listed below with their E number. E 200 E 201 E 202 E 203 E 210 E 211 E 212 E 213 E 214 E 215 E 216 E 217 E 218 E 219 E 220 E 221 E 222 E 223 E 224 E 226 E 227 E 228 E 230 E231 E 232 E233 E 235 E 236 E 237 E 238 E 239 E 249 E 250 E 251 E 252 E 28O E 281 E 282 E 283 E 290 Sorbic acid Sodium sorbate Potassium sorbate Calcium sorbate Benzoic acid Sodium benzoate Potassium benzoate Calcium benzoate Ethyl p-hydroxybenzoate Ethyl p-hydroxybenzoate Nasalt n-propyl p-hydroxybenzoate n-propyl p-hydroxybenzoate Na Salt Methyl p-hydroxybenzoate Methyl p-hydroxybenzoate Nasalt Sulfur dioxide Sodium sulfite Sodium hydrogensulfite Sodium disulfite Potassium disulfite Calcium sulfite Calcium hydrogensulfite Potassium hydrogensulfite Biphenyl (diphenyl) Orthophenylphenol Sodium orthophenylphenoxide Thiabendazole Natamycin Formic aci Sodium formate Calcium formate Hexamethylenetetramine Potassium nitrite Sodium nitrite Sodium nitrate Potassium nitrate Propionic acid Sodium propionate Calcium propionate Potassium propionate Carbon dioxide 0059 Also suitable according to the invention are pre servatives or preservative auxiliaries customary in cosmetics dibromodicyanobutane (2-bromo-2-bromomethylglutarod initrile), 3-iodo-2-propynyl butylcarbamate, 2-bromo-2-ni tropropane-1,3-diol, imidazolidinylurea, 5-chloro-2-methyl 4-isothiazolin-3-one, 2-chloroacetamide, benzalkonium chloride and benzyl alcohol. +formaldehyde donors Also suitable as preservatives are phenyl hydroxy alkyl ethers, in particular the compound known under the name phenoxyethanol on account of its bactericidal and fungicidal effects on a number of microorganisms Other antimicrobial agents are likewise suitable for being incorporated into the preparations according to the invention. Advantageous Substances are, for example, '-trichloro-2'-hydroxydiphenyl ether (irgasan), 1,6-di(4- chlorophenylbiguanido)hexane (chlorhexidine), 34,4'- trichlorocarbanilide, quaternary ammonium compounds, oil

33 US 2008/ A1 Mar. 27, 2008 of cloves, mint oil, thyme oil, triethyl citrate, farnesol (3,7,11-trimethyl-2,6,10-dodecatrien-1-ol), and the active ingredients or active ingredient combinations described in the patent laid-open specifications DE , DE , DE , DE , DE , DE , DE , DE , DE , DE , DE , DE , DE , DE , DE and DE and the patent specifications DE , DE , DE , DE , DE and DE Sodium hydrogencarbonate is also to be used advan tageously. Antimicrobial polypeptides can also likewise be used Suitable photofilter active ingredients are sub stances which absorb UV rays in the UV-B- and/or UV-A region. Suitable UV filters are, for example, 2,4,6-triaryl-1, 3.5-triazines in which the aryl groups may in each case carry at least one substituent which is preferably chosen from hydroxy, alkoxy, specifically methoxy, alkoxycarbonyl, spe cifically methoxycarbonyl and ethoxycarbonyl and mixtures thereof. Also suitable are p-aminobenzoic esters, cinnamic esters, benzophenones, camphor derivatives, and pigments which stop UV rays, such as titanium dioxide, talc and Zinc oxide Suitable UV filter substances are any UV-A and UV-B filter substances. The following examples may be mentioned: No. Substance CAS No. (=acid) 1 4-Aminobenzoic acid (4'-Trimethylammonium)benzylidenebornan-2-one methyl sulfate 3 3,3,5-Trimethylcyclohexyl salicylate (homosalate) 4 2-Hydroxy-4-methoxybenzophenone (oxybenzone) 5 2-Phenylbenzimidazole-5-sulfonic acid and its potassium, 27SO sodium and triethanolamine salts 6 3,3'-(1,4-Phenylenedimethine)bis(7,7-dimethyl oxobicyclo2.2.1]heptane-1-methanesulfonic acid) and its SaltS 7 Polyethoxyethyl 4-bis(polyethoxy)aminobenzoate 11301O Ethylhexyl 4-dimethylaminobenzoate Ethylhexyl salicylate Isoamyl 4-methoxycinnamate Ethylhexyl 4-methoxycinnamate S Hydroxy-4-methoxybenzophenone-5-sulfonic acid 4O (Sulisobenzone) and the sodium salt 13 3-(4'-Sulfobenzylidene)bornan-2-one and salts S8O3O Benzylidenebornan-2-one (4'-Isopropylphenyl)-3-phenylpropane-1,3-dione Isopropylbenzyl salicylate Imidazol-4-ylacrylic acid and its ethyl ester Ethyl 2-cyano-3,3-diphenylacrylate S '-Ethylhexyl 2-cyano-3,3-diphenylacrylate Menthyl O-aminobenzoate or: methyl-2-(1-methylethyl) 2-aminobenzoate 21 Glyceryl p-aminobenzoate or: glyceryl 4-aminobenzoate 22 2,2'-Dihydroxy-4-methoxybenzophenone (dioxybenzone) Hydroxy-4-methoxy-4-methylbenzophenone (mexenone) 24 Triethanolamine Salicylate Dimethoxyphenylglyoxalic acid or: ,4-dimethoxyphenylglyoxal acidic sodium 26 3-(4'-Sulfobenzylidene)bornan-2-one and its salts S tert-Butyl-4'-methoxydibenzoylmethane ,2'44'-Tetrahydroxybenzophenone S 29 2,2'-Methylenebis6-(2H-benzotriazol-2-yl)-4-(1,1,3, tetramethylbutyl)phenol 30 2,2'-(1,4-Phenylene)bis-1H-benzimidazole-4,6-18O disulfonic acid, Na Salt bis(4-(2-Ethylhexyloxy)-2-hydroxyphenyl (4-methoxyphenyl)-(1,3,5)-triazine 32 3-(4-Methylbenzylidene)camphor Polyethoxyethyl 4-bis(polyethoxy)paraaminobenzoate 11301O ,4-Dihydroxybenzophenone ,2'-Dihydroxy-4,4'-dimethoxybenzophenone-5,5' disodium Sulfonate 36 Benzoic acid, 2-4-(diethylamino)-2-hydroxybenzoyl, hexyl ester (2H-Benzotriazol-2-yl)-4-methyl-6-2-methyl-3-1,3,3,3-1SS tetramethyl-1-(trimethylsilyl)oxydisiloxanylpropylphenol 38 1,1-(2,2'-Dimethylpropoxy)carbonyl-4,4-diphenyl-1,3-butadiene

34 US 2008/ A1 Mar. 27, The cosmetic and dermatological preparations according to the invention may advantageously additionally comprise inorganic pigments which stop UV rays based on metal oxides and/or other metal compounds which are insoluble or slightly soluble in water and chosen from the group of oxides of zinc (ZnO), titanium (TiO), iron (e.g. Fe2O), Zirconium (ZrO2), silicon (SiO2), manganese (e.g. MnO), aluminum (Al2O), cerium (e.g. CeO), mixed oxides of the corresponding metals and mixtures of Such oxides The inorganic pigments can be present here in coated form, i.e. are surface-treated. This Surface treatment can consist, for example, in providing the pigments with a thin hydrophobic layer by a method known per se, as described in DE-A Suitable repellent active ingredients are com pounds which are able to repel or drive away certain animals, in particular insects, from humans. These include, for example, 2-ethyl-1,3-hexanediol, N,N-diethyl-m-tolua mide etc. Suitable hyperemic substances, which stimulate the flow of blood through the skin, are e.g. essential oils, Such as dwarf pine extract, lavender extract, rosemary extract, juniperberry extract, horse chestnut extract, birch leaf extract, hayflower extract, ethyl acetate, camphor, men thol, peppermint oil, rosemary extract, eucalyptus oil, etc. Suitable keratolytic and keratoplastic substances are, for example, salicylic acid, calcium thioglycolate, thioglycolic acid and its salts, sulfur, etc. Suitable antidandruff active ingredients are, for example, sulfur, Sulfur polyethylene glycol Sorbitan monooleate, Sulfur ricinol polyethoxylate, Zinc pyrithione, aluminum pyrithione, etc. Suitable antiin flammatory agents, which counteract skin irritations, are, for example, allantoin, bisabolol, dragosantol, camomile extract, panthenol, etc The cosmetic compositions according to the inven tion can comprise, as cosmetic and/or pharmaceutical active ingredient (and also if appropriate as auxiliary), at least one cosmetically or pharmaceutically acceptable polymer which differs from the polymers which form the polyelectrolyte complex used according to the invention. These include, quite generally, cationic, amphoteric and neutral polymers Suitable polymers are, for example, cationic poly mers with the INCI name Poly-quaternium, e.g. copolymers of vinylpyrrolidone/n-vinylimidazolium salts (Luviduat F C. Luvicquat HM, Luviduat MS, Luvicquat&commat, Care), copolymers of N-vinylpyrrolidone/dimethylaminoethyl methacrylate, quaternized with diethyl sulfate (Luviduat PQ 11), copolymers of N-vinylcaprolactam/N-vinylpyrrolidone/ N-vinylimidazolium salts (Luviduat E Hold), cationic cel lulose derivatives (Polyduaternium-4 and -10), acrylamido copolymers (Polyduaternium-7) and chitosan Suitable cationic (quaternized) polymers are also Merquat (polymer based on dimethyldiallylammonium chloride), Gafquat (quaternary polymers which are produced by the reaction of polyvinylpyrrolidone with quaternary ammonium compounds), Polymer JR (hydroxyethylcellu lose with cationic groups) and plant-based cationic poly mers, e.g. guar polymers such as the Jaguar grades from Rhodia Further suitable polymers are also neutral poly mers, such as polyvinylpyrrolidones, copolymers of N-vi nylpyrrolidone and vinyl acetate and/or vinyl propionate, polysiloxanes, polyvinylcaprolactam and other copolymers with N-vinylpyrrolidone, polyethyleneimines and salts thereof, polyvinylamines and salts thereof, cellulose deriva tives, polyaspartic acid salts and derivatives. These include, for example, Luviflex 0 Swing (partially saponified copoly mer of polyvinyl acetate and polyethylene glycol, BASF) Suitable polymers are also nonionic, water-soluble or water-dispersible polymers or oligomers, such as poly vinylcaprolactam, e.g. Luviskol 0 Plus (BASF), or polyvi nylpyrrolidone and copolymers thereof, in particular with vinyl esters, such as vinyl acetate, e.g. Luviskol 0 VA 37 (BASF), polyamides, e.g. based on itaconic acid and ali phatic diamines, as are described, for example, in DE-A Suitable polymers are also amphoteric or Zwitteri onic polymers, such as the octylacrylamide/methyl meth acrylate/tert-butylaminoethyl methacrylate/hydroxypropyl methacrylate copolymers obtainable under the names Amphomer (National Starch), and Zwitterionic polymers as are disclosed, for example, in the German patent applica tions DE , DE , DE and DE Acrylamidopropyltrimethylammonium chloride/ acrylic acid or methacrylic acid copolymers and alkali metal and ammonium salts thereof are preferred Zwitterionic poly mers. Further suitable Zwitterionic polymers are methacroyl ethylbetaine/methacrylate copolymers, which are available commercially under the name Amersette (AMERCHOL), and copolymers of hydroxyethyl methacrylate, methyl meth acrylate, N,N-dimethylaminoethyl methacrylate and acrylic acid (Jordapon (D)) Suitable polymers are also nonionic, siloxane-con taining, water-soluble or water-dispersible polymers, e.g. polyether siloxanes, such as Tegopren 0 (Goldschmidt) or Besis&commat (Wacker) The formulation base of pharmaceutical composi tions according to the invention preferably comprises phar maceutically acceptable auxiliaries. Pharmaceutically acceptable auxiliaries are those which are known for use in the field of pharmacy, food technology and related fields, in particular those listed in the relevant pharmacopeia (e.g. DAB Ph. Eur, BPNF) and other auxiliaries whose properties do not preclude a physiological application Suitable auxiliaries may be: lubricants, wetting agents, emulsifying and Suspending agents, preserving agents, antioxidants, antiirritatives, chelating agents, emul sion stabilizers, film formers, gel formers, odor-masking agents, resins, hydrocolloids, solvents, solubility promoters, neutralizing agents, permeation accelerators, pigments, qua ternary ammonium compounds, refatting and Superfatting agents, ointment, cream or oil base Substances, silicone derivatives, stabilizers, sterilizers, propellants, drying agents, opacifiers, thickeners, waxes, softeners, white oil. Formulation in this regard is based on specialist knowledge, as given, for example, in Fiedler, H. P. Lexikon der Hilf sstoffe für Pharmazie, Kosmetik und angrenzende Gebiete Lexicon of Auxiliaries for Pharmacy, Cosmetics and related fields, 4th ed., Aulendorf. ECV-Editio-Kantor-Verlag, To prepare the dermatological compositions according to the invention, the active ingredients can be mixed or diluted with a suitable auxiliary (excipient). Excipients may be solid, semisolid or liquid materials which can serve as a vehicle, carrier or medium for the active ingredient. Further auxiliaries are added, if desired, in the manner known to the person skilled in the art. In addition, the polymers and dispersions are suitable as auxiliaries in

35 US 2008/ A1 Mar. 27, 2008 pharmacy, preferably as or in coating(s) or binder(s) for Solid drug forms. They can also be used in creams and as tablet coatings and tablet binders According to a preferred embodiment, the compo sitions according to the invention are a skin-cleansing com position Preferred skin-cleansing compositions are soaps of liquid to gel-like consistency, such as transparent Soaps, luxury Soaps, deodorant Soaps, cream soaps, baby Soaps, skin protection soaps, abrasive soaps and Syndets, pasty Soaps, soft Soaps and washing pastes, exfoliating Soaps, moisturizing wipes, liquid washing, shower and bath prepa rations, such as washing lotions, shower baths and gels, foam baths, oil baths and scrub preparations, shaving foams, lotions and creams According to a further preferred embodiment, the compositions according to the invention are cosmetic com positions for the care and protection of the skin and hair, nail care compositions or preparations for decorative cosmetics Suitable skin cosmetic compositions are, for example, face tonics, face masks, deodorants and other cosmetic lotions. Compositions for use in decorative cos metics comprise, for example, concealing Sticks, stage makeup, mascara and eye shadows, lipsticks, kohl pencils, eyeliners, blushers, dusting powders and eyebrow pencils Furthermore, the polypeptide sequences (i) can be used in nose strips for pore cleansing, in antiacne compo sitions, repellents, shaving compositions, after-shave and pre-shave care compositions, aftersun care compositions, hair-removal compositions, hair colorants, intimate care compositions, foot care compositions, and in babycare The skincare compositions according to the inven tion are, in particular, W/O or O/w skin creams, day and night creams, eye creams, face creams, antiwrinkle creams, antisun creams, moisturizing creams, bleach creams, self tanning creams, vitamin creams, skin lotions, care lotions and moisturizing lotions Skin cosmetic and dermatological compositions based on the above-described poly-electrolyte complexes exhibit advantageous effects. The polymers can, inter alia, contribute to the moisturization and conditioning of the skin and to an improvement in the feel of the skin. The polymers can also act as thickeners in the formulations. By adding the polymers according to the invention, in certain formulations a considerable improvement in the skin compatibility can be achieved Skin cosmetic and dermatological compositions comprise preferably at least one polypeptide sequence (i) in an amount of from about to 30% by weight, preferably 0.01 to 20% by weight, very particularly preferably 0.1 to 12% by weight, based on the total weight of the composi tion Particularly photoprotective compositions based on the polypeptide sequences (i) have the property of increasing the residence time of the UV-absorbing ingredi ents compared to customary auxiliaries such as polyvi nylpyrrolidone. I0086) Depending on the field of use, the compositions according to the invention can be applied in a form Suitable for skincare, such as, for example, as a cream, foam, gel. Stick, mousse, milk, spray (pump spray or propellant-con taining spray) or lotion Besides the polypeptide sequences (i) and suitable carriers, the skin cosmetic preparations can also comprise further active ingredients and auxiliaries customary in skin cosmetics, as described above. These include preferably emulsifiers, preservatives, perfume oils, cosmetic active ingredients, such as phytantriol, Vitamin A, E and C, retinol, bisabolol, panthenol, photoprotective agents, bleaches, colo rants, tints, tanning agents, collagen, protein hydrolysates, stabilizers, ph regulators, dyes, salts, thickeners, gel form ers, consistency regulators, silicones, moisturizers, re-fatting agents and further customary additives. I0088 Preferred oil and fat components of the skin cos metic and dermatological compositions are the abovemen tioned mineral and synthetic oils, such as, for example, paraffins, silicone oils and aliphatic hydrocarbons having more than 8 carbon atoms, animal and vegetable oils, such as, for example, Sunflower oil, coconut oil, avocado oil, olive oil, lanolin, or waxes, fatty acids, fatty acid esters, such as, for example, triglycerides of the C6-C30-fatty acids, wax esters, such as, for example, jojoba oil, fatty alcohols, Vaseline, hydrogenated lanolin and acetylated lanolin, and mixtures thereof. I0089. The polypeptide sequences (i) according to the invention can also be mixed with conventional polymers if specific properties are to be established To establish certain properties, such as, for example, improvement in the feel to the touch, the spreading behavior, the water resistance and/or the binding of active ingredients and auxiliaries, such as pigments, the skin cos metic and dermatological preparations can additionally also comprise conditioning substances based on silicone com pounds Suitable silicone compounds are, for example, polyalkylsiloxanes, polyarylsiloxanes, polyarylalkylsilox anes, polyethersiloxanes or silicone resins The cosmetic or dermatological preparations are prepared by customary methods known to the person skilled in the art Preferably, the cosmetic and dermatological com positions are in the form of emulsions, in particular water in-oil (W/O) or oil-in-water (O/W) emulsions It is, however, also possible to choose other types of formulations, for example gels, oils, oleogels, multiple emulsions, for example in the form of W/O/W or O/W/O emulsions, anhydrous ointments or ointment bases, etc. Emulsifier-free formulations such as hydrodispersions, hydrogels or a Pickering emulsion are also advantageous embodiments The emulsions are prepared by known methods. Besides at least one polypeptide sequence (i), the emulsions generally comprise customary constituents, such as fatty alcohols, fatty acid esters and, in particular, fatty acid triglycerides, fatty acids, lanolin and derivatives thereof, natural or synthetic oils or waxes and emulsifiers in the presence of water. The selection of the additives specific to the type of emulsion and the preparation of Suitable emul sions is described, for example, in Schrader, Grundlagen und Rezepturen der Kosmetika Fundamentals and Formulations of Cosmetics, Hüthig Buch Verlag, Heidelberg, 2nd edition, 1989, third part, which is hereby expressly incorporated by reference A suitable emulsion as W/O emulsion, e.g. for a skin cream etc., generally comprises an aqueous phase which is emulsified by means of a suitable emulsifier system in an oil or fat phase. To provide the aqueous phase, a polyelectrolyte complex can be used.

36 US 2008/ A1 Mar. 27, Preferred fat components which may be present in the fatty phase of the emulsions are: hydrocarbon oils, such as paraffin oil, purcellin oil, perhydrosqualene and solutions of microcrystalline waxes in these oils; animal or vegetable oils, such as Sweet almond oil, avocado oil, calophylum oil, lanolin and derivatives thereof, castor oil, Sesame oil, olive oil, jojoba oil, karité oil, hoplostethus oil, mineral oils whose distillation start point under atmospheric pressure is about 250 C. and whose distillation end point is 410 C., such as, for example, Vaseline oil, esters of Saturated or unsaturated fatty acids, such as alkyl myristates, e.g. isopropyl, butyl or cetyl myristate, hexadecyl Stearate, ethyl or isopropyl palmi tate, octanoic or decanoic acid triglycerides and cetyl rici noleate The fatty phase can also comprise silicone oils soluble in other oils, such as dimethylpolysiloxane, meth ylphenylpolysiloxane and the silicone glycol copolymer, fatty acids and fatty alcohols Besides the polypeptide sequences (i) it is also possible to use waxes, such as, for example, carnauba wax, candelilla wax, beeswax, microcrystalline wax, ozokerite wax and Ca, Mg and Al oleates, myristates, linoleates and Stearates In addition, an emulsion according to the invention can be in the form of an O/W emulsion. Such an emulsion usually comprises an oil phase, emulsifiers which stabilize the oil phase in the water phase, and an aqueous phase, which is usually present in thickened form. Suitable emul sifiers are preferably O/W emulsifiers, such as polyglycerol esters, Sorbitan esters or partially esterified glycerides According to a further preferred embodiment, the compositions according to the invention are a shower gel, a shampoo formulation or a bath preparation Such formulations comprise at least one polypep tide sequence (i) and customary anionic Surfactants as base Surfactants and amphoteric and/or nonionic Surfactants as cosurfactants. Further Suitable active ingredients and/or aux iliaries are generally chosen from lipids, perfume oils, dyes, organic acids, preservatives and antioxidants, and thicken ersigel formers, skin conditioning agents and moisturizers. 0103) These formulations comprise preferably 2 to 50% by weight, preferably 5 to 40% by weight, particularly preferably 8 to 30% by weight, of surfactants, based on the total weight of the formulation In the washing, shower and bath preparations it is possible to use all anionic, neutral, amphoteric or cationic Surfactants customarily used in body-cleansing composi tions Suitable anionic surfactants are, for example, alkyl Sulfates, alkyl ether Sulfates, alkyl-sulfonates, alkylarylsul fonates, alkyl Succinates, alkyl SulfoSuccinates, N-alkoyl sarcosinates, acyl taurates, acyl isethionates, alkyl phos phates, alkyl ether phosphates, alkyl ether carboxylates, alpha-olefinsulfonates, in particular the alkali metal and alkaline earth metal salts, e.g. sodium, potassium, magne sium, calcium, and ammonium and triethanolamine salts. The alkyl ether sulfates, alkyl ether phosphates and alkyl ether carboxylates can have between 1 and 10 ethylene oxide or propylene oxide units, preferably 1 to 3 ethylene oxide units, in the molecule These include, for example, sodium lauryl sulfate, ammonium tauryt Sulfate, sodium lauryl ether Sulfate, ammonium lauryl ether sulfate, sodium lauryl Sarcosinate, Sodium oleyl Succinate, ammonium lauryl SulfoSuccinate, Sodium dodecylbenzenesulfonate, triethanolamine dodecyl benzenesulfonate Suitable amphoteric surfactants are, for example, alkylbetaines, alkylamidopropylbetaines, alkylsulfobe taines, alkyl glycinates, alkyl carboxyglycinates, alkyl amphoacetates or amphopropionates, alkyl amphodiacetates or amphodipropionates For example, cocodimethylsulfopropylbetaine, laurylbetaine, cocamidopropylbetaine or sodium cocam phopropionate can be used Suitable nonionic surfactants are, for example, the reaction products of aliphatic alcohols or alkylphenols hav ing 6 to 20 carbon atoms in the alkyl chain, which may be linear or branched, with ethylene oxide and/or propylene oxide. The amount of alkylene oxide is about 6 to 60 moles per mole of alcohol. In addition, alkylamine oxides, mono or dialkylalkanolamides, fatty acid esters of polyethylene glycols, ethoxylated fatty acid amides, alkyl polyglycosides or sorbitan ether esters are suitable Furthermore, the washing, shower and bath prepa rations can comprise customary cationic Surfactants, such as, for example, quaternary ammonium compounds, for example cetyltrimethylammonium chloride In addition, the shower gel/shampoo formulations can comprise thickeners, such as, for example, sodium chloride, PEG-55, propylene glycol oleate, PEG-120 meth ylglucose dioleate and others, and preservatives, further active ingredients and auxiliaries and Water According to a further preferred embodiment, the compositions according to the invention are a hair-treatment composition Hair-treatment compositions according to the invention preferably comprise at least one polypeptide sequence (i) in an amount in the range from about 0.01 to 30% by weight, preferably 0.5 to 20% by weight, based on the total weight of the composition Preferably, the hair-treatment compositions accord ing to the invention are in the form of a setting foam, hair mousse, hair gel, shampoo, hair spray, hair foam, end fluids, neutralizers for permanent waves, hair colorants and bleaches or hot-oil treatments. Depending on the field of use, the hair cosmetic preparations can be applied as (aerosol) spray, (aerosol) foam, gel, gel spray, cream, lotion or wax. Hair sprays here comprise both aerosol sprays and also pump sprays without propellant gas. Hair foams comprise both aerosol foams and also pump foams without propellant gas. Hair sprays and hair foams comprise preferably pre dominantly or exclusively water-soluble or water-dispers ible components. If the compounds used in the hair sprays and hair foams according to the invention are water-dispers ible, they can be applied in the form of aqueous microdis persions with particle diameters of from usually 1 to 350 nm, preferably 1 to 250 nm. The solids contents of these prepa rations here are usually in a range from about 0.5 to 20% by weight. These microdispersions generally require no emul sifiers or surfactants for their stabilization The hair cosmetic formulations according to the invention comprise, in a preferred embodiment, a) 0.01 to 30% by weight of at least one polypeptide sequence (i), b) 20 to 99.95% by weight of water and/or alcohol, c) 0 to 50% by weight of at least one propellant gas, d) 0 to 5% by weight of at least one emulsifier, e) 0 to 3% by weight of at least one thickener, and up to 25% by weight of further constituents.

37 US 2008/ A1 Mar. 27, Alcohol is understood as meaning all alcohols customary in cosmetics, e.g. ethanol, isopropanol, n-pro panol Further constituents are understood as meaning the additives customary in cosmetics, for example propellants, antifoams, inferface-active compounds, i.e. Surfactants, emulsifiers, foam formers and solubilizers. The interface active compounds used may be anionic, cationic, amphoteric or neutral. Further customary constituents may also be, for example, preservatives, perfume oils, opacifiers, active ingredients, UV filters, care substances, such as panthenol, collagen, Vitamins, protein hydrolysates, alpha- and beta hydroxycarboxylic acids, stabilizers, ph regulators, dyes, Viscosity regulators, gel formers, salts, moisturizers, re fatting agents, complexing agents and further customary additives These also include all styling and conditioner poly mers known in cosmetics which can be used in combination with the polypeptide sequences (i) according to the inven tion if very specific properties are to be established Suitable conventional hair cosmetic polymers are, for example, the above-mentioned cationic, anionic, neutral, nonionic and amphoteric polymers, which are hereby incor porated by reference To establish certain properties, the preparations can additionally also comprise conditioning Substances based on silicone compounds. Suitable silicone compounds are, for example, polyalkylsiloxanes, polyarylsiloxanes, polyaryla lkylsiloxanes, polyethersiloxanes, silicone resins or dime thicone copolyols (CTFA) and aminofunctional silicone compounds, such as amodimethicones (CTFA) The polymers according to the invention are par ticularly Suitable as setting agents in hair styling prepara tions, in particular hair sprays (aerosol sprays and pump sprays without propellant gas) and hair foams (aerosol foams and pump foams without propellant gas) In a preferred embodiment, spray preparations comprise a) 0.01 to 30% by weight of at least one polypep tide sequence (i), b) 20 to 99.9% by weight of water and/or alcohol, c) 0 to 70% by weight of at least one propellant, d) 0 to 20% by weight of further constituents Propellants are the propellants customarily used for hairsprays or aerosol foams. Preference is given to mixtures of propane?butane, pentane, dimethyl ether, 1,1-difluoroet hane (HFC-152 a), carbon dioxide, nitrogen or compressed a A formulation for aerosol hair foams preferred according to the invention comprises a) 0.01 to 30% by weight of at least one polypeptide sequence (i), b) 55 to 99.8% by weight of water and/or alcohol, c) 5 to 20% by weight of a propellant, d) 0.1 to 5% by weight of an emulsifier, e) 0 to 10% by weight of further constituents Emulsifiers which can be used are all of the emul sifiers customarily used in hair foams. Suitable emulsifiers may be nonionic, cationic or anionic or amphoteric Examples of nonionic emulsifiers (INCI nomen clature) are laureths, e.g. laureth-4, ceteths, e.g. cetheth-1, polyethylene glycol cetyl ethers, ceteareths, e.g. cetheareth 25, polyglycol fatty acid glycerides, hydroxylated lecithin, lactyl esters of fatty acids, alkyl polyglycosides Examples of cationic emulsifiers are cetyldim ethyl-2-hydroxyethylammonium dihydrogenphosphate, cetyltrimonium chloride, cetyltrimonium bromide, cocotri monium methyl sulfate, quaternium-1 to X (INCI). I0128 Anionic emulsifiers can, for example, be chosen from the group of alkyl sulfates, alkyl ether sulfates, alkyl Sulfonates, alkylarylsulfonates, alkyl Succinates, alkyl Sul fosuccinates, N-alkoylsarcosinates, acyl taurates, acyl isethionates, alkyl phosphates, alkyl ether phosphates, alkyl ether carboxylates, alpha-olefinsulfonates, in particular the alkali metal and alkaline earth metal salts, e.g. sodium, potassium, magnesium, calcium, and ammonium and tri ethanolamine salts. The alkyl ether sulfates, alkyl ether phosphates and alkyl ether carboxylates can have between 1 and 10 ethylene oxide or propylene oxide units, preferably 1 to 3 ethylene oxide units, in the molecule. I0129. A preparation suitable according to the invention for styling gels can, for example, have the following com position: a) 0.01 to 30% by weight of at least one polypep tide sequence (i), b) 80 to 99.85% by weight of water and/or alcohol, c) 0 to 3% by weight, preferably 0.05 to 2% by weight, of a gel former, d) 0 to 20% by weight of further constituents In general, the polypeptide sequences (i) used according to the invention already have a self-thickening effect, meaning that in many cases the use of gel formers can be dispensed with when preparing gels. Their use may, however, be advantageous in order to establish specific rheological or other application properties of the gels. Gel formers which may be used are all gel formers customary in cosmetics. These include slightly crosslinked polyacrylic acid, for example carbomer (INCI), cellulose derivatives, e.g. hydroxypropylcellulose, hydroxyethylcellulose, cationi cally modified celluloses, polysaccharides, e.g. Xanthan gum, caprylic/capric triglyceride, sodium acrylate copoly mers, polyduaternium-32 (and) Paraffinum Liquidum (INCI), sodium acrylate copolymers (and) Paraffinum Liq uidum (and) PPG-1 trideceth-6, acrylamidopropyltrimo nium chloride/acrylamide copolymers, steareth-10 allyl ether, acrylate copolymers, polyduaternium-37 (and) Paraf finum Liquidum (and) PPG-1 trideceth-6, polycuaternium 37 (and) propylene glycol dicaprate dicaprylate (and) PPG-1 trideceth-6, polyduaternium-7, polyduaternium-44. I0131 The polypeptide sequences (i) according to the invention can be used as conditioners in cosmetic prepara tions A preparation comprising the polypeptide sequences (i) according to the invention can preferably be used in shampoo formulations as setting agent and/or con ditioner. Preferred shampoo formulations comprise a) 0.01 to 30% by weight of at least one polypeptide sequence (i), b) 25 to 94.95% by weight of water, c) 5 to 50% by weight of surfactants, c) 0 to 5% by weight of a further conditioner, d) O to 10% by weight of further cosmetic constituents. I0133. In the shampoo formulations it is possible to use all of the anionic, neutral, amphoteric or cationic Surfactants customarily used in shampoos. I0134) Suitable anionic surfactants are, for example, alkyl sulfates, alkyl ether sulfates, alkylsulfonates, alkylarylsul fonates, alkyl Succinates, alkyl SulfoSuccinates, N-alkoylsar cosinates, acyl taurates, acyl isethionates, alkyl phosphates, alkyl ether phosphates, alkyl ether carboxylates, alpha olefinsulfonates, in particular the alkali metal and alkaline earth metal salts, e.g. sodium, potassium, magnesium, cal cium, and ammonium and triethanolamine salts. The alkyl ether sulfates, alkyl ether phosphates and alkyl ether car

38 US 2008/ A1 Mar. 27, 2008 boxylates can have between 1 and 10 ethylene oxide or propylene oxide units, preferably 1 to 3 ethylene oxide units, in the molecule Of suitability are, for example, sodium lauryl sul fate, ammonium lauryl Sulfate, Sodium lauryl ether Sulfate, ammonium lauryl ether Sulfate, sodium lauroyl sarcosinate, Sodium oleyl Succinate, ammonium lauryl SulfoSuccinate, Sodium dodecylbenzenesulfonate, triethanolamine dodecyl benzenesulfonate Suitable amphoteric surfactants are, for example, alkylbetaines, alkylamidopropyl-betaines, alkylsulfobe taines, alkyl glycinates, alkyl carboxyglycinates, alkyl amphoacetates or amphopropionates, alkylamphodiacetates or amphodipropionates For example, cocodimethylsulfopropylbetaine, laurylbetaine, cocamidopropylbetaine or sodium cocam phopropionate can be used Suitable nonionic surfactants are, for example, the reaction products of aliphatic alcohols or alkylphenols hav ing 6 to 20 carbon atoms in the alkyl chain, which may be linear or branched, with ethylene oxide and/or propylene oxide. The amount of alkylene oxide is about 6 to 60 moles per mole of alcohol. In addition, alkylamine oxides, mono or dialkylalkanolamides, fatty acid esters of polyethylene glycols, alkyl polyglycosides or Sorbitan ether esters are suitable Furthermore, the shampoo formulations can com prise customary cationic Surfactants, such as, for example, quaternary ammonium compounds, for example cetyltrim ethylammonium chloride In the shampoo formulations, customary condition ers can be used in combination with the polypeptide sequences (i) to achieve certain effects These include, for example, the abovementioned cationic polymers with the INCI name Polyduaternium, in particular copolymers of vinylpyrrolidone/n-vinylimidazo lium salts (Luviduat FC, Luvicquat&commat, HM, Luviduat MS, Luviduat Care), copolymers of N-vinylpyrrolidone/ dimethylaminoethyl methacrylate, quaternized with diethyl sulfate (Luviduat D PO 11), copolymers of N-vinylcapro lactam/n-vinylpyrrolidone/n-vinylimidazolium salts (Luvi quat D Hold), cationic cellulose derivatives (Polyduater nium-4 and -10), acrylamide copolymers (Polyduaternium 7). In addition, protein hydrolysates can be used, and conditioning Substances based on silicone compounds, for example polyalkylsiloxanes, polyarylsiloxanes, polyaryla lkylsiloxanes, polyethersiloxanes or silicone resins. Further Suitable silicone compounds are dimethicone copolyols (CTFA) and aminofunctional silicone compounds such as amodimethicones (CTFA). In addition, cationic guar deriva tives, such as guar hydroxypropyltrimonium chloride (INCI) can be used The invention further relates to keratin-binding effector molecules consisting of (i) at least one polypeptide sequence which has a binding affinity for a keratin, (ii) an effector molecule which is not naturally linked to the polypeptide sequence (i) Suitable polypeptide sequences (i) are described above A particular advantageous embodiment of the invention are polypeptide sequences (i) which include at least one of the following polypeptide sequences, 0145 i. the polypeptide sequence (domain B) 0146 ii. the polypeptide sequence (domain C) 0147 iii. a polypeptide sequence which is modified com pared with (a) in up to 70% of the amino acids, 0148 iv. a polypeptide sequence which is modified com pared with (b) in up to 70% of the amino acids, with the proviso that the keratin binding of polypeptide sequence (c) or (d) amounts to at least 10% of the value shown by polypeptide sequence (a) or (b), measured in the assay described in example 9 or 10. Domain B or C means in this connection the keratin-binding domains, described above and on the following pages, of human desmoplakin (SEQID NO: 1). Modification of amino acids thereby means amino acid Substitutions, insertions and deletions or any combinations of these three possibilities Polypeptide sequences (i) preferably used are those having a highly specific affinity for the desired organism. Accordingly, for applications in skin cosmetics, the polypep tide sequences (i) preferably employed are those having a particularly high affinity for the keratin of human skin. The polypeptide sequences preferred for applications in hair cosmetics are those having a particularly high affinity for the keratin of human hair For applications in the pet sector, correspondingly, the preferred polypeptide sequences (i) are those having a particularly high affinity for the corresponding keratin, for example canine keratin or feline keratin However, it is also possible to use more than one polypeptide sequence (i) in the effector molecule of the invention, for example a sequence (i) which has a high binding affinity for the keratin of human skin, in conjunction with a sequence (i) which has a high affinity for the keratin of human hair. It is also possible for a plurality of copies of the same polypeptide sequence (i) to be connected consecu tively in order, for example, to achieve higher binding Suitable keratin-binding polypeptide sequences (i) are known. For example, desmoplakins and plectins com prise keratin-binding domains. (Fontao L. Favre B. Riou S, Geerts D, Jaunin F. Saurat J. H. Green KJ, Sonnenberg A. Borradori L., Interaction of the bullous pemphigoid antigen 1 (BP230) and desmoplakin with intermediate filaments is mediated by distinct sequences within their COOH termi nus., Mol Biol Cell May: 14(5): Epub 2003 Jan. 26; Hopkinson S. B. Jones J C. The N terminus of the transmembrane protein BP180 interacts with the N-terminal domain of BP230, thereby mediating keratin cytoskeleton anchorage to the cell Surface at the site of the hemidesmo some, Mol Biol Cell January; 11(1):277-86) It is possible for such regions to be mapped and identified by alignments of Such known protein sequences, for example using a computer program Such as Vector NTI 8 (Version of Sep. 25, 2002) supplied by InforMax Inc Further suitable polypeptide sequences (i) with good binding to human keratin are sequence regions which show high homology or sequence identity in an alignment and can be regarded as consensus sequences of the keratin binding domains. (O155 Particular preference is sequence regions to the following: given among these domain B (KBD-B): polypeptide sequence SEQ ID NO: 1 position 2193 to 2448 domain B (KBD-B): polypeptide sequence SEQ ID NO: 1 position 2209 to 2448

39 US 2008/ A1 11 Mar. 27, 2008 domain C (KBD-C): polypeptide sequence SEQ ID NO: 1 position 2606 to 2871 domain C (KBD-C): polypeptide sequence SEQ ID NO: 1 position 2616 to 2871 domain C (KBD-C): polypeptide sequence SEQ ID NO: 1 position 2616 to 2811 domain C (KBD-C): polypeptide sequence SEQ ID NO: 1 position 2606 to If it is desired that the polypeptide sequences (i) have particularly good binding to a keratin from a non human organism, the sequence motifs selected as Suitable will preferably be those from the keratin-binding protein, e.g. desmoplakin or plectin, of the appropriate organism FIG. 2 shows an alignment of keratin-binding molecules. Effector Molecules (ii) 0158 Effector molecules (ii) mean hereinafter molecules which have a particular, predictable effect. They may be either proteinaceous molecules such as enzymes or else non-proteinogenic molecules such as dyes, Sunscreens, Vita mins, provitamins, antioxidants and fatty acids, condition ers, or metal ion-containing compounds Among the proteinaceous effector molecules, pref erence is given to enzymes and antibodies Among the enzymes, the following are preferred as effector molecules (ii): oxidases, peroxidases, proteases, glucanases, mutanase, tyrosinases, laccases, metal-binding enzymes, lactoperoxidase, lysozyme, amyloglycosidase, glucose oxidase, Superoxide dismutase, photolyase, T4 endonuclease, catalase, thioredoxin, thioredoxin reductase. The proteinaceous effector molecules (ii) without enzymatic activity which are preferred as effector molecules (ii) are the following: antimicrobial peptides, silk proteins, hydro phobins, collaten, carotenoid-binding proteins, heavy metal binding proteins, odorant-binding proteins Also very suitable as proteinaceous effector mol ecules (ii) are hydrolysates of proteins from vegetable and animal sources, for example hydrolysates of proteins of marine origin or silk hydrolysates Among the non-proteinaceous effector molecules (ii), preference is given to dyes, for example food dyes, semipermanent dyes or reactive or oxidation dyes. In the case of oxidation dyes, it is preferred for one component to be coupled as effector molecule (ii) to the keratin-binding polypeptide sequence (i) and then be oxidatively coupled to the second dye component at the site of action, i.e. after binding to the hair. It is further preferred with oxidation dyes to carry out the coupling of the color components before the linkage to the polypeptide sequence (i) The reactive dyes may further preferably be linked as one component as effector molecule (ii) to the keratin binding polypeptide sequence (i) and then be bound to the hair. It is further possible for such dyes which are linked as effector molecule (ii) to the keratin-binding polypeptide sequence (i) to be employed in decorative cosmetics through binding to nails or skin Suitable dyes for the molecules of the invention are all conventional hair dyes. Suitable dyes are known to the skilled worker from handbooks of cosmetics, for example Schrader, Grundlagen und Rezepturen der Kosmetika, Hüthig Verlag, Heidelberg, 1989, ISBN Particularly advantageous dyes are those specified in the list below. The colour index numbers (CIN) are taken from the Rowe Colour Index, 3" edition, Society of Dyers and Colourists, Bradford, England, Chemical name or other name CIN Color Pigment Green Acid Green 1 2,4-Dinitrohydroxynaphthalene-7-sulfonic acid Pigment Yellow 1 Pigment Yellow 3 Pigment Orange 1 2,4-Dihydroxyazobenzene Solvent Red 3 -(2'-Chloro-4'-nitro-1'-phenylazo)-2-hydroxynaphthalene Pigment Red 3 Ceres Red: Sudan Red: Fat Red G Pigment Red 112 Pigment Red 7 Pigment Brown 1 4-(2-Methoxy-5'-sulfodiethylamido-1'-phenylazo)-3-hydroxy-5'- O006 green 0020 green O316 yellow 1680 yellow 1710 yellow 1725 orange 1920 orange 2010 re. 2O85 re re re re. 242O re brown 2490 re. chloro-2',4'-dimethoxy-2-naphthanilide Disperse Yellow yellow -(4-Sulfo-1-phenylazo)-4-aminobenzene-5-sulfonic acid 3015 yellow 2,4-Dihydroxyazobenzene-4'-sulfonic acid 4270 orange 2-(2,4-Dimethylphenylazo-5-sulfo)-1-hydroxynaphthalene-4-sulfonic 4700 re acid 2-(4-Sulfo-1-naphthylazo)-1-naphthol-4-sulfonic acid 472O re 2-(6-Sulfo-2,4-xylylazo)-1-naphthol-5-sulfonic acid 4815 re 1-(4'-Sulfophenylazo)-2-hydroxynaphthalene 5510 orange 1-(2-Sulfo-4-chloro-5-carboxy-1-phenylazo)-2- SS25 re. hydroxynaphthalene 1-(3-Methylphenylazo-4-sulfo)-2-hydroxynaphthalene SS80 re. 1-(4'.(8)-Sulfonaphthylazo)-2-hydroxynaphthalene 562O re. 2-Hydroxy-1,2-azonaphthalene-1'-sulfonic acid 5630 re. 3-Hydroxy-4-phenylazo-2-naphthylcarboxylic acid 58OO re. 1-(2-Sulfo-4-methyl-1-phenylazo)-2-naphthylcarboxylic acid S8iSO re.

40

41 US 2008/ A1 13 Mar. 27, continued Chemical name or other name 1,2-Dioxyanthraquinone, calcium-aluminum complex 3-Oxypyrene-5,8,10-sulfonic acid 1-Hydroxy-4-N-phenylaminoanthraquinone 1-Hydroxy-4-(4-methylphenylamino)anthraquinone Acid Violet 23 1,4-Di(4'-methylphenylamino)anthraquinone 1,4-Bis(O-sulfo-p-toluidino)anthraquinone Acid Blue 80 Acid Blue 62 N,N'-Dihydro-1,2,1',2'-anthraquinone azine Vat Blue 6: Pigment Blue 64 Vat Orange 7 indigo indigo disulfonic acid 44-Dimethyl-6,6'-dichlorothioindigo 5,5'-Dichloro-77-dimethylthioindigo Quinacridone Violet 19 Pigment Red 122 Pigment Blue 16 Phthalocyanine Direct Blue 86 Chlorinated phthalocyanine Natural Yellow 6, 19: Natural Red 1 Bixin, nerbixin Lycopene trans-alpha-, beta- or gamma-caroteine Keto and/or hydroxyl derivatives of carotene Guanine or pearlescent agent,7-bis(4-hydroxy-3-methoxyphenyl)-1,6-heptadiene-3,5-dione Complex salt (Na, Al, Ca) of carminic acid Chlorophylla and b; copper compounds of chlorophylls and chlorophyllins Aluminum Hydrated alumina Hydrous aluminosilicates Oltramarine Blue Pigment Red 101 and 102 Barium sulfate Bismuth oxychloride and its mixtures with mica Calcium carbonate Calcium sulfate Carbon Black Pigment Black 9 Medicinal charcoal, vegetable carbon Chromium oxide Chromium oxide hydrate Pigment Blue 28, Pigment Green 14 Pigment Metal 2 Gold ron oxides and hydroxides ron oxide ron oxide hydrate ron oxide Mixtures of iron(ii) and iron(iii) hexacyanoferrate Pigment white 18 Manganese ammonium diphosphate Manganese phosphate, Mn(PO)27H2O Silver Titanium dioxide and its mixtures Zinc oxide 6,7-Dimethyl-9-(1'-D-ribityl)isoalloxazine, lactoflavin Caramel Capsanthin, capsorubin Betanin Benzopyrylium salts, anthocyanins Bromocresol Green Aluminum, zinc, magnesium, and calcium Stearates Bromothymol Blue Acid Red 195 CIN Color red green violet violet violet green green blue blue blue blue orange blue 7301S be red violet violet red blue blue blue green yellow orange yellow orange yellow white yellow red green white white white ble 7701S red white white white white black black black green green green brown brown orange red yellow black 77S10 ble white violet red white white white yellow brown Orange red red green white blue red

42 US 2008/ A1 Mar. 27, Also very suitable as hair dyes are food dyes The abovementioned dyes can also be used as effector molecules (ii) to a skin- or nail-binding polypeptide sequence (i) for the coloring of skin or nails e.g. in tattoos The effector molecule (ii) which are linked to the keratin-binding polypeptide sequence (i) are also, if desired, easily be separated from the keratin in skin, hair or nail again. For this purpose it is possible to employ for example washing with keratin, whereby effector molecule (ii) which are linked to the keratin-binding polypeptide sequence (i) are displaced from their existing binding to the keratin and are Saturated with the keratin from the washing solution. Alternatively, a washing with a high content of detergent (e.g. SDS) is also possible for the washing out. (0169. Further preferred effector molecules (ii) are fatty acids, in particular saturated fatty acids carrying an alkyl branch, particularly preferably branched eicosanoic acids, Such as 18-methyleicosanoic acid Further preferred effector molecules (ii) are caro tenoids. According to the invention, carotenoids are under stood as meaning the following compounds and esterified or glycosylated derivatives thereof. B-carotene, lycopene, lutein, astaxanthin, Zeaxanthin, cryptoxanthin, citranaxan thin, canthaxanthin, bixin, 3-apo-4-carotenal, B-apo-8-caro tenal, 3-apo-8-carotenoic esters, neurosporene, echinenone, adonirubin, violaxanthin, torulene, torularhodin, singly or as mixture. Carotenoids which are preferably used are B-caro tene, lycopene, lutein, astaxanthin, Zeaxanthin, citranaxan thin and canthaxanthin Further preferred effector molecules (ii) are vita mins, especially vitamin A and esters thereof Retinoids mean for the purposes of the present invention vitamin Aalcohol (retinol) and its derivatives such as vitamin A aldehyde (retinal), Vitamin A acid (retinoic acid) and vitamin A esters (e.g. retinyl acetate, retinyl propionate and retinyl palmitate). The term retinoic acid includes in this connection both all-trans-retinoic acid and 13-cis-retinoic acid. The terms retinol and retinal preferably include the all-trans compounds. The retinoid preferably used for the Suspensions of the invention is all-trans-retinol, referred to as retinol hereinafter. (0173. Further preferred effector molecules (ii) are vita mins, provitamins and vitamin precursors from the A, C, E and F groups, especially 3,4-didehydroretinol, B-carotene (provitamin of vitamin A), ascorbic acid (vitamin C), and the palmitic esters, glucosides or phosphates of ascorbic acid, tocopherols, especially C-tocopherol and its esters, e.g. the acetate, the nicotinate, the phosphate and the Succinate; additionally vitamin F, by which are meant essential fatty acids, especially linoleic acid, linolenic acid and arachidonic acid The vitamins, provitamins or vitamin precursors of the vitamin B group or derivatives thereof, and the deriva tives of 2-furanone which are preferably to be employed according to the invention include, inter alia: 0175 Vitamin B, trivial name thiamine, chemical name 3-(4-amino-2'-methyl-5'-pyrimidinyl) methyl-5-(2-hy droxyethyl)-4-methylthiazolium chloride Vitamin B, trivial name riboflavin, chemical name 7,8-dimethyl-10-(1-D-ribityl)-benzoglpteridine-2,4(3H, 1OH)-dione. Riboflavin occurs in free form for example in whey, and other riboflavin derivatives can be isolated from bacteria and yeasts. A riboflavin stereoisomer which is likewise suitable according to the invention is lyxoflavin which can be isolated from fish meal or liver and which has a D-arabityl radical in place of D-ribity Vitamin B. The compounds nicotinic acid and nicotinamide (niacinamide) are frequently designated thus. Nicotinamide is preferred according to the invention Vitamin B (pantothenic acid and panthenol). Pan thenol is preferably employed. Panthenol derivatives which can be employed according to the invention are, in particu lar, the esters and ethers of panthenol, and cationically derivatized panthenols. In a further preferred embodiment of the invention it is possible to employ in addition to pan tothenic acid or panthenol also derivatives of 2-furanone. Particularly preferred derivatives are the substances, which are also commercially available, dihydro-3-hydroxy-4.4- dimethyl-2(3h)-furanone with the trivial name pantolactone (Merck), 4-hydroxymethyl-y-butyrolactone (Merck), 3.3- dimethyl-2-hydroxy-y-butyrolactone (Aldrich) and 2,5-di hydro-5-methoxy-2-furanone (Merck), with all stereoiso mers being expressly included These compounds advantageously confer moistur izing and skin-soothing properties on the keratin-binding effector molecules of the invention Vitamin B by which is meant not a uniform substance but the derivatives of 5-hydroxymethyl-2-meth ylpyridin-3-ol which are known under the trivial names of pyridoxine, pyridoxamine and pyridoxal Vitamin B, (biotin), also referred to as vitamin H or skin vitamin'. Biotin is (3aS, 4S, 6aR)-2-oxohexahy drothienol 3,4-dimidazole-4-valeric acid Panthenol, pantolactone, nicotinamide and biotin are very particularly preferred according to the invention It is possible according to the invention to use Suitable derivatives (salts, esters, Sugars, nucleotides, nucleosides, peptides and lipids). Preferred lipophilic, oil soluble antioxidants from this group are tocopherol and its derivatives, gallic esters, flavonoids and carotenoids, and butylated hydroxytoluenel/anisole. Preferred water-soluble antioxidants are amino acids, e.g. tyrosine and cysteinee and derivatives thereof, and tannins especially those of vegetable origin Triterpenes, especially triterpene acids such as ursolic acid, rosmarinic acid, betulinic acid, boswellic acid and bryonolic acid A further preferred effector molecule is lipoic acid and Suitable derivatives (salts, esters, Sugars, nucleotides, nucleosides, peptides and lipids) Further preferred effector molecules (ii) are UV light filters. By this are meant organic Substances able to absorb ultraviolet rays and emit the absorbed energy again in the form of longer-wavelength radiation, e.g. heat. The organic Substances may be oil-soluble or water-soluble Examples of oil-soluble UV-B filters which can be used are the following Substances: benzylidenecamphor and its derivatives, e.g. 3-(4-methylbenzylidene)camphor; aminobenzoic acid derivatives, preferably 2-eth ylhexyl 4-(dimethylamino)benzoate, 2-octyl 4-(dimethy lamino)benzoate and amyl 4-(dimethylamino)benzoate; esters of cinnamic acid, preferably 2-ethylhexyl 4-meth oxycinnamate, propyl 4-methoxycinnamate, isoamyl 4-methoxycinnamate, isopentyl 4-methoxycinnamate, 2-ethylhexyl 2-cyano-3-phenylcinnamate (octocrylene);

43 US 2008/ A1 15 Mar. 27, esters of salicylic acid, preferably 2-ethylhexyl Salicylate, 4-isopropylbenzyl salicylate, homomethyl sali cylate; 0191 derivatives of benzophenone, preferably 2-hy droxy-4-methoxybenzophenone, 2-hydroxy-4-methoxy 4'-methylbenzophenone, 2,2'-dihydroxy-4-methoxyben Zophenone; esters of benzalmalonic acid, preferably 2-ethyl hexyl 4-methoxybenzalmalonate; 0193 triazine derivatives such as, for example, trianilino-(p-carbo-2'-ethyl-1'-hexyloxy)-1,3,5-triazine (octyl triazone) and dioctylbutamido triazone (Uvasorb(R) HEB): 0194 propane-1,3-diones such as, for example, 1-(4-tert butylphenyl)-3-(4-methoxyphenyl)propane-1,3-dione Suitable water-soluble substances are: phenylbenzimidazole-5-sulfonic acid and the alkali metal, alkaline earth metal, ammonium, alkylam monium, alkanolammonium and glucammonium salts thereof 0197) sulfonic acid derivatives of benzophenone, prefer ably 2-hydroxy-4-methoxybenzophenone-5-sulfonic acid and its salts; 0198 sulfonic acid derivatives of 3-benzylidenecamphor Such as, for example, 4-(2-oxo-3-bornylidenemethyl)ben Zenesulfonic acid and 2-methyl-5-(2-oxo-3-bornylidene) sulfonic acid and salts thereof It is particularly preferred to use esters of cinnamic acid, preferably 2-ethylhexyl 4-methoxycinnamate, isopen tyl 4-methoxycinnamate, 2-ethylhexyl 2-cyano-3-phenyl cinnamate (octocrylene) It is further preferred to use derivatives of ben Zophenone, in particular 2-hydroxy-4-methoxybenzophe none, 2-hydroxy-4-methoxy-4-methylbenzophenone, 2,2'- dihydroxy-4-methoxybenzophenone and to use propane-1, 3-diones such as, for example 1-(4-tert-butylphenyl)-3-(4- methoxyphenyl)propane-1,3-dione Typical UV-A filters which are suitable are: 0202 derivatives of benzoylmethane such as, for example, 1-(4'-tert-butylphenyl)-3-(4-methoxyphenyl) propane-1,3-dione, 4-tert-butyl-4'-methoxydibenzoyl methane or 1-phenyl-3-(4-isopropylphenyl)propane-1,3- dione; 0203 amino-hydroxy-substituted derivatives of ben Zophenones such as, for example, N,N-diethylaminohy droxybenzoyl-n-hexyl benzoate The UV-A and UV-B filters can, of course, also be employed in mixtures Further suitable UV filter substances are given in the table below. No. Substance CAS No. (=acid) 1 4-Aminobenzoic acid (4'-Trimethylammonium)benzylidenebornan-2-one methyl sulfate 3 3,3,5-Trimethylcyclohexyl salicylate Hydroxy-4-methoxybenzophenone (oxybenzone) 5 2-Phenylbenzimidazole-5-sulfonic acid and its potassium, 27SO (homosalate) sodium and triethanolamine salts 6 and its 3,3'-(1,4-Phenylenedimethine)bis(7,7-dimethyl- 2-oxobicyclo2.2.1]heptane-1-methanesulfonic acid) SaltS 7 Polyethoxyethyl 4-bis(polyethoxy)aminobenzoate 11301O Ethylhexyl 4-dimethylaminobenzoate Ethylhexyl salicylate Isoamyl 4-methoxycinnamate Ethylhexyl 4-methoxycinnamate S Hydroxy-4-methoxybenzophenone-5-sulfonic acid 4O (Sulisobenzone) and the sodium salt 13 3-(4'-Sulfobenzylidene)bornan-2-one and salts S8O3O Benzylidenebornan-2-one (4'-Isopropylphenyl)-3-phenylpropane-1,3-dione Isopropylbenzyl salicylate Imidazol-4-ylacrylic acid and its ethyl ester Ethyl 2-cyano-3,3-diphenylacrylate S '-Ethylhexyl 2-cyano-3,3-diphenylacrylate Menthyl O-aminobenzoate or: methyl-2-(1-methylethyl) 2-aminobenzoate 21 Glyceryl p-aminobenzoate or: glyceryl 4-aminobenzoate 22 2,2'-Dihydroxy-4-methoxybenzophenone (dioxybenzone) Hydroxy-4-methoxy-4-methylbenzophenone (mexenone) 24 Triethanolamine Salicylate Dimethoxyphenylglyoxalic acid or: ,4-dimethoxyphenylglyoxal acidic sodium 26 3-(4'-Sulfobenzylidene)bornan-2-one and its salts S tert-Butyl-4'-methoxydibenzoylmethane ,2'44'-Tetrahydroxybenzophenone S 29 2,2'-Methylenebis6-(2H-benzotriazol-2-yl)-4-(1,1,3,3- tetramethylbutyl)phenol

44 US 2008/ A1 16 Mar. 27, 2008 No. Substance -continued 30 2,2'-(1,4-Phenylene)bis-1H-benzimidazole-4,6- disulfonic acid, Na Salt 31 2,4-bis(4-(2-Ethylhexyloxy)-2-hydroxyphenyl 6-(4-methoxyphenyl)-(1,3,5)-triazine 32 3-(4-Methylbenzylidene)camphor 33 Polyethoxyethyl 4-bis(polyethoxy)paraaminobenzoate 34 2,4-Dihydroxybenzophenone 35 2,2'-Dihydroxy-4,4'-dimethoxybenzophenone-5,5'- disodium sulfonate 36 Benzoic acid, 2-4-(diethylamino)-2-hydroxybenzoyl, hexyl ester 37 2-(2H-Benzotriazol-2-yl)-4-methyl-6-2-methyl-3-1,3,3,3- tetramethyl-1-(trimethylsilyl)oxydisiloxanylpropylphenol CAS No. (=acid) 18O O SS Besides the two aforementioned groups of primary photoprotective substances it is also possible to employ secondary Sunscreens of the antioxidant type which break the chain of photochemical reactions which is induced when UV rays penetrate into the skin. Typical examples thereof are Superoxide dismutase, catalase, tocopherols (vitamin E) and ascorbic acid (vitamin C) A further group are anti-irritants which have an anti-inflammatory effect on skin damaged by UV light. Examples of Such substances are bisabolol, phytol and phytantriol. Linkage of the Effector Molecules (ii) to the Keratin Binding Polypeptide Sequence (i) The effector molecules (ii) are connected to a polypeptide sequence (i) which has a binding affinity for a keratin. The connection between (i) and (ii) can be both a covalent bond and based on ionic or van der Waals interac tions A covalent linkage is preferred. This can take place for example via the side chains of the polypeptide sequence (i), in particular via amino functions or hydroxyl functions or carboxylate functions or thiol functions. Linkage via the amino functions of one or more lysine residues, one or more thiol groups of cysteine residues or via the N-terminal or C-terminal function of the polypeptide (i) is preferred. Apart from the amino acid functions present in the polypeptide sequence (i) it is also possible for amino acids with Suitable functions (e.g. cysteines, lysines, aspartates, glutamates) to be attached to the sequence or for amino acids of the polypeptide sequence (i) to be substituted by Such amino acid functions Linkage of the effector molecules (ii) to the polypeptide sequence (i) can take place either directly, i.e. as covalent linkage of two chemical functions already present in (i) and (ii), for example an amino function of (i) is linked to a carboxylate function of (ii) to give the amide. The linkage can, however, also take place via a so-called linker, i.e. an at least bifunctional molecule, which undergoes bonding with one function to (i) and is linked by one or more other functions to (ii) If the effector molecule (ii) likewise consists of a polypeptide sequence, the linkage of (i) and (ii) can take place through a so-called fusion protein, i.e. a continuous polypeptide sequence consisting of the two partial sequences (i) and (ii) It is also possible to incorporate so-called spacer elements between (i) and (ii), for example polypeptide sequences which have a potential cleavage site for a pro tease, lipase, esterase, phosphatase, hydrolase, or oligo- and polypeptide sequences which allow the fusion protein to be purified easily, for example so-called His tags, i.e. oligohis tidine residues The spacer elements may further be composed of alkyl chains, ethylene glycol and polyethylene glycols Particularly preferred linker and/or spacer elements have a potential cleavage site for a protease, lipase, esterase, phosphatase, hydrolase, i.e. are enzymatically cleavable. Examples of enzymatically cleavable linkers which can be used in the molecules according to the invention are given, for example, in WO 98/01406, to the entire contents of which reference is hereby expressly made Particularly preferred linkers and spacers are ther mally cleavable, photocleavable. Corresponding chemical structures are known to the person skilled in the art and are integrated between the molecular moieties (i) and (ii) Linkage in the case of a non-proteinaceous effector molecule to the polypeptide sequence (i) preferably takes place with functionalizable residues (side groups, C or N terminus) on the polypeptide (i) which undergo covalent connection to the chemical function of the effector molecule The linkage in this case is preferably via an amino, thiol or hydroxyl function of the polypeptide (i), which are able to undergo a corresponding amide, thioester or ester bonding for example with a carboxyl function of the effector molecule (ii), where appropriate after activation A further preferred linkage of the polypeptide sequence (i) to an effector molecule (ii) is the use of a tailored linker. Such a linker has two or more so-called anchor groups with which it can link the polypeptide sequence (i) and one or more effector molecules (ii). For example, an anchor group for (i) may be a thiol function by means of which the linker can undergo disulfide bonding to a cysteine residue of the polypeptide (i). An anchor group for (ii) may be for example a carboxyl function by means of which the linker can undergo ester bonding to a hydroxyl function of the effector molecule (ii) The use of such tailored linkers allows the linkage to be adapted accurately to the desired effector molecule. It is additionally possible thereby to link a plurality of effector molecules to a polypeptide sequence (i) in a defined manner The linker which is used depends on the function ality to be coupled. Suitable examples are molecules which

45 US 2008/ A1 Mar. 27, 2008 couple to polypeptides (i) by means of Sulfhydryl-reactive groups, e.g. maleimides, pyridyl disulfides, C-haloacetyls, vinyl sulfones, sulfatoalkyl sulfones (preferably sulfatoethyl sulfones) and to effector molecules (ii) by means of 0221 Sulfhydryl-reactive groups (e.g. maleimides, pyridyl disulfides, C-haloacetyls, vinyl Sulfones, sulfa toalkyl sulfones (preferably sulfatoethyl sulfones) 0222 amine-reactive groups (e.g. Succinimidyl esters, carbodiimides, hydroxymethylphosphine, imidoesters, PFP esters etc.) 0223 Sugars or oxidized Sugar-reactive groups (e.g. hydrazides etc.) 0224 carboxy-reactive groups (e.g. carbodiimides etc.) 0225 hydroxyl-reactive groups (e.g. isocyanates etc.) 0226 thymine-reactive groups (e.g. psoralen etc.) 0227 nonselective groups (e.g. aryl azides etc.) 0228 photoactivatable groups (e.g. perfluorophenyl azide etc.) 0229 metal-complexing groups (e.g. EDTA, hexahis, ferritin) 0230 antibodies and fragments thereof (e.g. single chain antibodies, F(ab) fragments of antibodies, cata lytic antibodies) An alternative possibility is direct coupling between active substance/effector and the keratin-binding domain, e.g. by means of carbodiimides, glutaraldehyde, the abovementioned crosslinkers or other crosslinkers known to the skilled worker The keratin-binding effector molecules of the invention can also, if desired, easily be separated from the keratin again. It is possible to employ for this purpose for example washing with keratin, whereby the keratin-binding effector molecules are displaced from their existing binding to the keratin and are saturated with the keratin from the washing solution. Reversible adhesion of a plurality of effector molecules to keratin is thus possible. Alternatively, a washing with a high content of detergent (e.g. SDS) is possible for the washing out The keratin-binding effector molecules of the invention have a wide area of application in human cosmet ics, especially in skin and hair care, animal care, leather care and leather processing The keratin-binding effector molecules of the invention are preferably used for skin, nail and hair cosmet ics. They permit a high concentration and long duration of action of skin-, nail- and hair-care or skin-, nail- and hair-protecting effectors Suitable auxiliaries and additives for producing hair cosmetic or skin cosmetic preparations are familiar to the skilled worker and can be found in handbooks of cosmetics, for example Schrader, Grundlagen und Rezep turen der Kosmetika, Hüthig Verlag, Heidelberg, 1989, ISBN In a further embodiment, this hair cosmetic or skin cosmetic preparation serves to care for or protect the skin or hair and is the form of an emulsion, a dispersion, a Suspen Sion, an aqueous Surfactant preparation, a milk, a lotion, a cream, a balsam, an ointment, a gel, a granulation, a dusting powder, a stick product such as, for example, a lipstick, a foam an aerosol or a spray. Such formulations are very Suitable for topical preparations. Suitable emulsions are oil-in-water emulsions and water-in-oil emulsions or micro emulsions The hair cosmetic or skin cosmetic preparation is ordinarily used for application to the skin (topically) or hair. Topical preparations mean in this connection preparations which are suitable for applying the active Substances to the skin in fine distribution and preferably in a form which can be absorbed through the skin. Examples suitable for this purpose are aqueous and hydroalcoholic Solutions, sprays, foams, foam aerosols, ointments, aqueous gels, emulsions of the O/W or W/O type, microemulsions or cosmetic stick products In a preferred embodiment of the cosmetic com position of the invention, the composition comprises a carrier. A preferred carrier is water, a gas, a water-based liquid, an oil, a gel, an emulsion or microemulsion, a dispersion or a mixture thereof. Said carriers are well tolerated by skin. Particularly advantageous for topical preparations are aqueous gels, emulsions or microemul S1O.S Emulsifiers which can be used are nonionic sur factants, Zwitterionic Surfactants, ampholytic Surfactants or anionic emulsifiers. The emulsifiers may be present in the composition of the invention in amounts of from 0.1 to 10, preferably 1 to 5, 96 by weight based on the composition It is possible to use as nonionic surfactant for example a surfactant from at least one of the following groups: adducts of 2 to 30 mol of ethylene oxide and/or 0 to 5 mol of propylene oxide with linear fatty alcohols having 8 to 22 C atoms, with fatty acids having 12 to 22 C atoms and with alkylphenols having 8 to 15 C atoms in the alkyl group; Cs fatty acid monoesters and diesters of adducts of 1 to 30 mol of ethylene oxide with glycerol: 0241 glycerol monoesters and diesters and sorbitan monoesters and diesters of Saturated and unsaturated fatty acids having 6 to 22 carbon atoms and their ethylene oxide adducts; alkyl mono- and oligoglycosides having 8 to 22 carbon atoms in the alkyl radical and their ethoxylated analogs; adducts of 15 to 60 mol of ethylene oxide with castor oil and/or hardened castor oil; polyol esters and especially polyglycerol esters such as, for example, polyglycerol polyricinoleate, polyglycerol poly 12-hydroxy Stearate or polyglycerol dimerate. Likewise Suit able are mixtures of compounds from a plurality of these Substance classes; adducts of 2 to 15 mol of ethylene oxide with castor oil and/or hardened castor oil; partial esters based on linear, branched, unsaturated or saturated C2 fatty acids, ricinoleic acid and 12-hydroxys tearic acid and glycerol, polyglycerol, pentaerythritol, dipentaerythritol, Sugar alcohols (e.g. Sorbitol), alkyl gluco sides (e.g. methyl glucoside, butyl glucoside, lauryl gluco side) and polyglucosides (e.g. cellulose); mono-, di- and trialkyl phosphates and mono-, di- and/or tri-peg-alkyl phosphates and the salts thereof; wool wax alcohols; polysiloxane-polyalkyl polyether copolymers and corre sponding derivatives; mixed esters of pentaerythritol, fatty acids, citric acid and fatty alcohol as disclosed in DE and/or mixed

46 US 2008/ A1 Mar. 27, 2008 esters of fatty acids having 6 to 22 carbon atoms, methyl glucose and polyols, preferably glycerol or polyglycerol, and polyalkylene glycols; betaines Zwitterionic surfactants can also be used as emul sifiers. The surface-active compounds referred to as Zwitte rionic Surfactants are those having at least one quaternary ammonium group and at least one carboxylate or one sulfonate group in the molecule. Particularly suitable Zwit terionic Surfactants are the so-called betaines such as the N-alkyl-N,N-dimethylammonium glycinates, for example the cocoalkyldimethyl-ammonium glycinate, N-acylamino propyl-n,n-dimethylammonium glycinates, for example the cocoacylaminopropyldimethylammonium glycinate; and 2-alkyl-3-carboxylmethyl-3-hydroxyethylimidazolines each having 8 to 18 C atoms in the alkyl or acyl group, and the cocoacylaminoethylhydroxyethylcarboxymethyl glycinate. A particularly preferred fatty amide derivative is that known under the CTFA name cocamidopropyl betaine Emulsifiers which are likewise suitable are ampholytic Surfactants. Ampholytic Surfactants means Sur face-active compounds which, apart from a Css-alkyl or -acyl group, comprise at least one free amino group and at least one COOH or - SOH group in the molecule and are able to form inner salts. Examples of suitable ampholytic Surfactants are N-alkylglycines, N-alkylpropionic acids, N-alkylaminobutyric acids, N-alkyliminodipropionic acids, N-hydroxyethyl-N-alkylamidopropylglycines, N-alkyltau rines, N-alkylsarcosines, 2-alkylaminopropionic acids and alkylaminoacetic acids each having about 8 to 18 C atoms in the alkyl group Particularly preferred ampholytic surfactants are N-cocoalkylaminopropionate, cocoacylaminoethylamino propionate and Cis-acylsarcosine. Besides the ampholytic emulsifiers, also Suitable are quarternary emulsifiers, with particular preference for those of the ester quat type, pref erably methyl-quaternized di-fatty acid triethanolamine ester salts. Anionic emulsifiers which can also be employed are alkyl ether Sulfates, monoglyceride Sulfates, fatty acid Sulfates, SulfoSuccinates and/or ether carboxylic acids Suitable oily substances are guerbet alcohols based on fatty alcohols having 6 to 18, preferably 8 to 10, carbon atoms, esters of linear C-C fatty acids with linear C-C, fatty alcohols, esters of branched C-C carboxylic acids with linear C-C fatty alcohols, esters of linear C-C, fatty acids with branched alcohols, especially 2-ethylhex anol, esters of linear and/or branched fatty acids with polyhydric alcohols (such as, for example, propylene glycol, dimerdiol or trimertriol) and/or guerbet alcohols, triglycer ides based on C-C fatty acids, liquid mono/di-, triglyc eride mixtures based on C-Cls fatty acids, esters of C-C, fatty alcohols and/or guerbet alcohols with aromatic car boxylic acids, especially benzoic acid, esters of C-C2 dicarboxylic acids with linear or branched alcohols having 1 to 22 carbon atoms or polyols having 2 to 10 carbon atoms and 2 to 6 hydroxyl groups, vegetable oils, branched primary alcohols, substituted cyclohexanes, linear C-C fatty alco hol carbonates, guerbet carbonates, esters of benzoic acid with linear and/or branched C-C alcohols (e.g. Finsolv(R) TN), dialkyl ethers, ring-opened products of epoxidized fatty acid esters with polyols, silicone oils and/or aliphatic or naphthenic hydrocarbons. Further oily substances which can be employed are silicone compounds, for example dimeth ylpolysiloxanes, methylphenylpolysiloxanes, cyclic sili cones and amino-, fatty acid-, alcohol-, polyether-, epoxy-, fluorine-, alkyl- and/or glycoside-modified silicone com pounds which may at room temperature be both in liquid form and in the form of a resin. The oily substances may be present in the compositions of the invention in amounts of from 1 to 90, preferably 5 to 80, and in particular 10 to 50, % by weight based on the composition The duration of action on the skin can be signified prolonged by coupling appropriate compounds to a keratin binding polypeptide (i). The coupling takes place as described above, and formulation and application take place by methods known to the skilled worker. Effector molecules (ii) suitable in particular for deodorants are: perfume oils, cyclodextrines, ion exchangers, Zinc ricinoleate, antimicro bial/bacteriostatic compounds (e.g. DCMX, Irgasan DP300, TCC) Suitable for antipersipirants are: tannins, and Zinc? aluminum salts A further area of application of the substances of the invention is the therapeutic or prophylactic use for certain disorders of the skin and of the mucous membranes. It is advantageous, especially in the oral, pharyngeal and nasal spaces, for active Substances for therapy/prophylaxis to be bound more strongly and for a longer time via a keratin-binding domain. Areas of application thereofare, in particular: 0249 viral diseases (e.g. herpes, coxsackie, varicella Zoster, cytomegalovirus etc) 0250 bacterial diseases (e.g. TB, syphilis etc.) 0251 fungal diseases (e.g. candida, cryptococcus, his toplasmosis, aspergillus, mucormycosis etc.) 0252 neoplastic diseases (e.g. melanomas, adenomas etc.) 0253) autoimmune diseases (e.g. PEMPHIGUS VUL GARIS, BULLOUS PEMPHIGOID, SYSTEMIC LUPUS ERYTHEMATOSIS etc.) 0254 sunburn 0255 parasitic infestation (e.g. ticks, mites, fleas etc.) 0256 insect contact (e.g. blood-sucking insects such as anopheles etc.) 0257 The substances suitable for therapy or prophylaxis (e.g. corticoids, immunosuppressant compounds, antibiot ics, antimycotics, antiviral compounds, insect repellent etc.) can be coupled via the linkers described above (a linker to be optimized according to the functionality to be coupled) to the keratin-binding polypeptides (i). EXAMPLE 1. Expression Vectors and Production Strains 0258 Various expression vectors were tested for the expression of the keratin-binding domains (KBD). For this, various promoters were used (e.g. IPTG-inducible, rham nose-inducible, arabinose-inducible, methanol-inducible, constitutive promoters, etc.). Constructs were likewise tested in which the KBD were expressed as fusion proteins (e.g. as fusion with thioredoxin, or egfp, or YaaD B. subtilis, SWISS-PROT: P37527, PDX1, etc.). Here, both the described KBD-B (keratin-binding domain B), and KBD-C (keratin-binding domain C), and the combination of the two domains KBD-BC were expressed using the various expression systems. The vector constructs mentioned are nonlimiting for the claim.

47 US 2008/ A1 Mar. 27, Given by way of representative as an example is the vector map of the IPTG-inducible vectorpoe30-kbd-b (FIG. 3), of the methanol-inducible vectors plib 15 (FIG. 4) and plib16 (FIG. 5), and of the inducible vector plib19 (FIG. 6). The procedure for KBD-C may also be analogous to the described vector constructions and expressions For the expression of the KBD, various production hosts were used, such as, for example, E. coli strains (see Ex. 2: e.g. XL10-Gold Stratagene. BL21-CodonPlus Strat agene, and others). However, other bacterial production hosts, such as, for example, Bacillus megaterium or Bacillus subtilis, were also used. In the case of the KBD expression in B. megaterium, the procedure was carried out analogously to: Barg, H., Malten, M. & Jahn, D. (2005). Protein and Vitamin production in Bacillus megaterium. In Methods in Biotechnology-Microbial Products and Biotransformations (Barredo, J.-L., ed.) The fungal production strains used were Pichia pastoris (see Ex. 3; e.g. GS115 and KM71 both from Invitrogen; and others) and Aspergillus nidulans (see Ex. 4; e.g. RMS011 Stringer, M A. Dean, R A, Sewall, T C. Timberlake, W E (1991) Rodletless, a new Aspergillus developmental mutant induced by direct gene activation. Genes Dev 5: und SRF200 Karos, M, Fischer, R (1999) Molecular characterization of Hyma, an evolution arily highly conserved and highly expressed protein of Aspergillus nidulans. Mol Genet Genomics 260: , and others). However, it is also possible to use other fungal production hosts, such as, for example, Aspergillus niger (KBD expression analogous to EP A1 and/or WO 98/46772) for the KBD expression. EXAMPLE 2 KBD Expression in E. coli Strains with IPTG Inducible Promoters, e.g. by the Expression Plas mid pcoe30-kbd-b 0262 For the expression, various production hosts were used. Such as, for example, various E. coli strains (e.g. XL10-Gold Stratagene, BL21-CodonPlus Stratagene. and others), Bacillus megaterium, Bacillus subtilis etc Described here by way of representation as an example is the cloning and expression of KBD-B by E. coli, transformed with poe30-kbd-b: Cloning of pqe30-kbd-b Lambda-MaxiDNA (DNA-Lambda Maxi Kit, Qiagen) was prepared from a cdna bank of human keratinocytes (BD Bioscience, Clontech, Human Kera tinocyte cdna, foreskin, primary culture in log phase, vector: Wigt11) The PCR was carried out using the following oligonucleotides: Bag 43 (5' - GGTCAGTTACGTGCAGCTGAAGG -3') and Bag 44 (5' - GCTGAGGCTGCCGGATCG -3') 0266 The resulting PCR product about 1102 bp in size was cut out of an agarose gel and purified Using the purified PCR product as template, a 2nd PCR was then carried out: 0268 Oligonucleotides used: Bag 53 : (5' - CGCGCCTCGAGCCACATACTGGTCTGC -3") and Bag 51 (5' - GCTTAGCTGAGGCTGCCGGATCG -3') The resulting PCR product about 1073 bp in size was cut out of an agarose gel, purified and cloned in the following vector: pcr2.1-topo (Invitrogen). (0270. The resulting vector pcr2.1-topo--kbd-b (5027 bp) was then transformed, amplified in E. coli, then cleaved with XhoI and EcoRI and the resulting KBD-B fragment was cloned in prad/his A (Invitro gen; likewise cleaved with XhoI and EcoRI). (0271 The newly formed vector pbad/his A+KBD-B (5171 bp) was again cleaved with SacI and StuI and the resulting KBD-B fragment was cloned in pcre30 (Qiagen; cleaved with SacI and SmaI). The resulting expression vector pge30-kbd-b (4321 bp; see also FIG. 3) was used for the following KBD-B expressions. (0272. The KBD-B expressed by the vector pqe30 KBD-B in E. coli additionally included, on the N-terminus, besides the polypeptide sequence SEQ ID NO: 1 position , the amino acids MRGSHHHHHHGSACEL, and, on the C-terminus, the amino acids GVDLQPSLIS. (0273 Expression of KBD-B by poe30-kbd-b in E. coli 0274 Precultures were inoculated from plate or glyc erol culture with poe30-kbd-b transformed E. coli strains (e.g. XL 10-Gold Stratagene). Depending on the size of the main culture, inoculation with LB medium (about 1:100) was carried out in a tube or a Small flask Antibiotics were used according to the strain used (for pge30-kbd-b amplicillin 100 ug/ml) Incubation was carried out at 250 rpm and 37 C. (0277. The main culture was inoculated about 1:100 with preculture, main culture: LB medium or suitable minimal medium with the respective antibiotics. Incu bation at 250 rpm and 37 C Induction was carried out with 1 mm IPTG above an OD (600 nm) of After induction for 4 h, the cells were centri fuged off In fermenters the procedure was analogous, although it was possible to carry out induction at much higher OD units and thus to considerably increase the cell and protein yield. EXAMPLE 3 Intracellular and Secretory Expression of KBD by Means of Pichia pastoris Strains Using Methanol Inducible Promoters, e.g. Through the Expression Plasmids plib 15 and plib 16 (shaking flask) 0281 For the KBD expression, various Pichia pastoris strains were used, such as, for example, GS115 and KM71 (Pichia Expression Kit, Version M: Invitrogen Life Tech nologies) Described here is by way of representative as an example the expression of KBD-B by P. pastoris, trans

48 US 2008/ A1 20 Mar. 27, 2008 formed with plib 15 (intracellular expression, vector see FIG. 4) or plib 16 (secretory expression, vector see FIG. 5). (0283 For the construction of plib15, a KBD-B-en coding DNA fragment about 930 bp in size was ampli fied by means of PCR using the oligonucleotides Lib148 (5'-GCTAAGGAATTCACCATGCATCAC CATCACCATCACGAGCCACATACTGGTC TGCT 3') and Lib149 (5'-GCTGGAGAAMTTCT CAGCTAATTAAGCTTGGCTGCA-3"), and the vector poe30-kbd-b (Example 2, FIG. 3) as tem plates. Here, EcoRI restriction sites were introduced at both ends of the PCR products For the construction of plib16, a KBD-B-en coding DNA fragment about 930 bp in size was ampli fied by means of PCR using the oligonucleotides Lib149 (5'-GCTGGAGAATTCTCAGCTAAT TAAGCTTGGCTGCA-3') and Lib150 (5'-GCTAAG GAATTCCATCACCATCACCATCACGAGC CACATACTGGTCTGCT-3") and the vector pge30 KBD-B (Example 2, FIG. 3) as templates. Here, EcoRI restriction sites were introduced at both ends of the PCR products. (0285) The PCR product which was amplified with the oligonucleotides Lib148/Lib 149 was digested with EcoRI and ligated into the EcoRI-cleaved vector ppic3.5 (Pichia Expression Kit, Version M, Invitro gen). The correct KBD-B amplification was checked by sequencing the vector plib15 (FIG. 4) resulting from the ligation. (0286. The PCR product which was amplified with the oligonucleotides Lib149/Lib 150 was digested with EcoRI and ligated into the EcoRI-cleaved vector ppic9 (Pichia Expression Kit, Version M, Invitrogen). The correct KBD-B amplification was checked by sequenc ing the vector plib 16 (FIG. 5) resulting from the ligation Electrocompetent cells and spheroplasts of the P. pastoris strains were transformed with the circular and StuI-linearized vectors plib 15 and plib The transformants were analyzed by means of PCR and Southern blotting using chromosomal DNA For the preculture, KBD-B-expressing P. pas toris transformants were inoculated from plate or glyc erol culture. Depending on the size of the main culture, inoculation with MGY, BMG or BMGY medium (Pi chia-expression-kit, Version M, Invitrogen) (about 1:100) was carried out in a tube or a small flask The culture was incubated at rpm and 30 C. until ODoo The cells were harvested with xg for 5 min at room temperature For the main culture, the harvested cell pellet was taken up at an ODoo-1 in methanol-comprising mm, BMM or BMMY medium (Pichia-Expression Kit, Version M, Invitrogen) in order to induce the expression The main culture was incubated at rpm and 30 C. for 1-96 h The induction was maintained every 24 h by adding 100% methanol at a methanol end concentration of 0.5% In the case of intracellular expression, the har vesting and disruption of the cells was carried out after the end of the main culture by means of a Menton Gaulin In the case of secretory expression, the culture supernatant was collected and the KBD-B was purified from it directly The KBD-B expressed intracellularly in P. pas toris (plib15) included, besides the polypeptide sequence SEQID NO: 1 position , addition ally, at the N-terminus, the amino acids MHHHHHH, and, at the C-terminus, the amino acids GVDLOPSLIS The KBD-B expressed secretorily in P. pastoris (plib16) included, prior to processing, besides the polypeptide sequence SEQ ID NO: 1 position , additionally at the N-terminus the amino acids MRFPSIFTAVLFMSSALAAPVNTTTEDE TAQIPAEAVIGYSDLEGDFDVAVLPFS NST NNGLLFINTTIASIAAKEEGVSLEKRE AEAYVEFHHHHHH, and, at the C-terminus, the amino acids GVDLQPSLIS The KBD-B processed and secreted by means of P. pastoris (plib16) included, besides the polypeptide sequence SEQID NO: 1 position , addition ally at the N-terminus the amino acids YVEFHHH HHH, and at GVDLQPSLIS. the C-terminus the amino acids EXAMPLE 4 Expression of KBD by Means of Aspergillus nidu lans Strains Using the Inducible alca Promoter, e.g. Through the Expression Plasmid plib 19 (Shaking Flask) 0300 For the expression, A. nidulans wild type strains were used, such as, for example, RMS011 or SRF200. Described here is by way of representation as an example the expression of KBD-B by A. nidulans, trans formed with plib19 (FIG. 6) For the construction of plib 19, a KBD-B-en coding DNA fragment about 900 bp in size was ampli fied by means of PCR using the oligonucleotides Lib151 (5'-CACCATGCATCACCATCACCATCAC GAGCCACATACTGGTCTGCT-3") and Lib152 (5-GCTAATTAAGCTTGGCTGCA-3"), and the vector pqe30-kbd-b (Example 2, FIG. 3) as template. The PCR product was ligated into the vector pentr/d (pentrtm Directional TOPOR) Cloning Kit, Version E, Invitrogen). The correct KBD-B amplification was checked by sequencing. 0302) The recombination of the KBD-B encoding DNA fragment was carried out into the vector pmt OvE (Toews M. W. Warmbold J. Konzack S, Rischitor P. Veith D, Vienken K, Vinuesa C, Wei H, Fischer R: Establishment of mrfp1 as a fluorescent marker in Aspergillus nidulans and construction of expression vectors for high-throughput protein tagging using recombination in vitro (GATEWAY). (2004) Curr Genet 45: ) using the Gateway(R) LR Clo nasetm enzyme mix' (Invitrogen). This produced the vector plib19 (FIG. 6) Protoplasts of the A. nidulans wild type strains were transformed with the circular vector plib19. The transformants were analyzed by means of PCR and Southern blotting using chromosomal DNA.

49 US 2008/ A1 Mar. 27, For the preculture of KBD-B-expressing A. nidulans transformants, 100 ml of minimal medium (0.6% NaNO; 0.152% KHPO; 0.052% KCl ph 6.5; 0.8% glucose: 0.05% MgSO; 1 ml trace element solution 1 g/l FeSOax,HO; 8.8 g/l ZnSOax,HO: 0.4 g/l CuSOXHO: 0.15 g/l MnSOXHO; 0.1 g/1 NaBO7x1OHO; 0.05 g/l (NH4)Mo,OxH2O). +strain-specific supplements) or 100 ml of complete medium (2% malt extract; 0.1% peptone; 2% glucose: +strain-specific supplements) were inoculated in 500 ml flasks with spores and incubated for h at rpm and 37 C After the preculture, the fungal mycelium was harvested by filtration, washed with distilled water and transferred to flasks with ml of fresh minimal medium. In this main culture medium, 0.1% fructose was used instead of glucose as the C-source. To induce the KBD expression, ethanol (1% final concentration) or glycerol (50 mm) or sodium acetate (50 mm) or ethylamine or threonine were additionally added to the medium. The additives mentioned for inducing the expression are not limiting for the claim. The main culture was incubated for a further 5-48 h at rpm and 37 C After the end of the culture, the fungal mycelium was harvested with xg for 5 min at room temperature and disrupted by means of a Menton Gaulin. (0307 Besides the polypeptide sequence SEQ ID NO: 1 position , the KBD-B expressed in A. nidulans (plib19) additionally included, at the N-ter minus, the amino acids MHHHHHH, and, at the C-ter minus, the amino acids KGGRADPAFLYKW MIRLLTKPERKLLEGGPGTQLLFPLVRVNCALG VIMVIAVS CVKLLSAHNSTOHTSRKHKV. EXAMPLE 5 Cell Disruption and Inclusion Body Purification poe30-kbd-b 0308 Solubly expressed KBD could be used directly following purification. Insolubly expressed KBD (e.g. in inclusion bodies) was purified as follows: 0309 The fermenter was centrifuged, the pellet was suspended in 20 mm phosphate buffer ph-7.4 and disrupted by means of a Menton-Gaulin The disrupted cells were centrifuged again ( g), the pellet from this was treated with 20 mm phosphate, 500 mm NaCl and 8 Murea and so stirred. (Dissolution of the Inclusion Bodies) The ph of the supernatant was adjusted to Centrifugation was then carried out again and the Supernatant was applied to an Nichelate Sepharose column. EXAMPLE 6 Purification of Keratin-Binding Domain B on Ni Chelate Sepharose 0313 The KBD could be purified chromatographically through the attached His tag over an Nicolumn Column material: Ni-Sepharose High Performance 0315 Amersham Biosciences order No.: The material was packed into a column (e.g. diam eter 2.6 cm, height 10 cm) and equilibrated with buffer A+4% buffer B (corresponds to 20 mm imidazole) The protein extract (see e.g. cell disruption and inclusion body purification) was applied to the column at ph 7.5 using a Superloop (AKTA system) (flow about 5 ml/min) Following application, washing was carried out with buffer A+20 mm imidazole Elution was carried out with buffer B (500 mm imidazole in buffer A) The eluate was collected in fractions using a frac tion collector. Buffer A: 20 mm sodium dihydrogenphosphate mm NaCl Murea 0323 ph=7.40 Buffer B: 20 mm sodium dihydrogenphosphate mm NaCl Murea mm imidazole 0327 ph=740 EXAMPLE 7 Renaturation of Keratin-Binding Domain B Insolubly expressed keratin-binding domain (e.g. from inclusion bodies) can be renatured and thus activated as follows: Method 1: Discontinuous Dialysis ml of Cellytic IB (Sigma, order No. C5236) and 5 mm DTT were added to 6.5 ml of KBD-B inclusion bodies in 8 Murea (Nichelate eluate, HiTrap). The solution to be renatured was then poured into a dialysis tube (Spectrum: Spectra Por MWCO:12-14 kd) Carry out dialysis for about 12 hours against 1 L of 6 Murea solution at 4 C. with careful stirring ml of 25 mm Tris/HCl ph=7.50 were added and dialysis was carried out like this for 9 hours at 4 C. Subsequent addition of a further 250 ml of the Tris buffer (see above) and dialysis for a further 12 hours ml of 25 mm Tris/HC1 ph=7.50 were then added again and dialysis was carried out like this for 9 hours at 4 C. Subsequent addition of a further 250 ml of the Tris buffer (see above) and dialysis for a further 12 hours ml of 25 mm Tris/HC1 ph=7.50 were then added again and dialysis was carried out like this for 9 hours at 4 C. The dialysis tube containing the dialyzate was then placed into 2L: 25 mm Tris+150 mm. NaCl ph=7.50. Dialysis was then carried out again at 4 C. for 12 hours The contents of the dialysis tube were then removed. Method 2: Continuous Dialysis ml of KBD-B inclusion bodies in 8 Murea (Ni chelate eluate, HiTrap) were treated with 10 ml of Cellytic IB (Sigma, order No. C5236) and 5 mm DTT. The solution was then poured into a dialysis chamber: Slide-A-Lyzer Dialyses Cassette PIERCE, MWCO: 10 kd. Order No.: Dialysis was then carried out for about 1 hour against 1 L 6 Murea solution at 4 C.

50 US 2008/ A1 22 Mar. 27, Then, over a period of 48 h, 2 1 of the following buffer were metered in continuously by means of a peristal tic pump: 25 mm Tris/HCl ph The dialysis tube containing the dialyzate was then added to 2 1 of the end buffer: 25 mm Tris+150 mm NaCl ph-7.50 and dialysis was carried out for about 12 hours at 4 C The contents of the dialysis tube were then removed. EXAMPLE 8 Binding to Skin 1 (Qualitative) 0340 A visual qualitative test was developed in order to examine whether KBD binds to skin. Solutions Used: (0341 Blocking solution: DIG Wash+Buffer set Boehringer MA (10x solution) diluted in TBS. TBS: 20 mm Tris; 150 mm NaCl ph 7.5 TTBS: TBS-0.05% Tween2O The first step is the transfer of the outer keratin layer of the skin to a stable support. For this purpose, a transparent adhesive tape is firmly applied to depilated human skin and removed again. The test can be carried out directly on the transparent adhesive strip, or the adhering keratin layer can be transferred to a glass slide through renewed adhesion. Binding was demonstrated as follows: 0343 For incubation with the various reagents, trans fer to a Falcon vessel 0344 If appropriate addition of ethanol for degreasing, removal of ethanol and drying of the slide 0345 Incubation with blocking buffer for 1 h at room temperature (0346 2x washing for 5 min with TTBS (0347 1x washing for 5 min with TBS (0348 Incubation with the KBD to be tested (coupled to tag e.g. His HA etc.) or control protein in TBS/0. 05% Tween 20 for 2-4 hat room temperature 0349 Removal of the supernatant x washing with TBS Incubation for 1 h at room temperature with monoclonal anti-polyhistidine (or specific KBD rabbit) antibodies, diluted 1:2000 in TBS+0.01% blocking x washing for 5 min with TTBS x washing for 5 min with TBS 0354) Incubation for 1 h at room temperature with anti-mouse IgG alkaline-phosphatase conjugate, diluted 1:5000 in TBS+0.01% blocking x washing for 5 min with TTBS 0356) 1x washing for 5 min with TBS 0357 Addition of phosphatase substrate (NBT-BCIP: Boehringer MA 1 tablet/40 ml of water 2.5 min; stop: with water) 0358 Optical detection of the colored precipitate with the naked eye or using a microscope. A blue colored precipitate indicates that KBD has bound to the skin. EXAMPLE 9 Binding to Skin 2 (Quantitative) 0359 A quantitative test was developed with which the hair/skin binding strength of the KBD can be compared with nonspecific proteins A5 mm cork borer was used to bore a section out of a thawed dry piece of skin without hair (human or pig) (or in the case of a surface test a section of skin is inserted into a Falcon lid). The sample of skin was then brought to a thickness of 2-3 mm in order to remove any tissue present. The skin sample was then transferred to an Eppendorf vessel (protein low-bind) in order to carry out the binding demon stration (see also FIG. 7): 0361) 2x washing with PBS/0.05% Tween Addition of 1 ml of 1% BSA in PBS and incubation for 1 h at room temperature, gentle Swirling movements (900 rpm) Removal of the supernatant Addition of 100 ug of KBD in PBS with 0.05% Tween 20; incubation for 2 hat room temperature and gentle Swimming movements (900 rpm) Removal of the supernatant x washing with PBS/0.05% Tween Incubation with 1 ml of monoclonal mouse anti-tag (His6 or HA or specific KBD) antibodies with peroxidase conjugate (1:2000 in PBS with 0.05% Tween 20) Monoclonal AntipolyHistidine Peroxidase Conjugate, produced in mouse, lyophilized powder, Sigma for 2-4 h at room temperature, gentle Swirling movement (900 rpm) x washing with PBS/0.05% Tween Addition of peroxidase substrate (1 ml/eppen dorf vessel; composition see below) 0370 Allow reaction to run until a blue coloration (about 90 seconds) Stop the reaction with 100 ul of 2 um HSO The absorption was measured at 405 nm. Peroxidase Substrate (Prepare Shortly Beforehand): ml TMB solution (42 mm TMB in DMSO) +10 ml substrate buffer (0.1 M sodium acetate ph 4.9) ul H2O 3% strength EXAMPLE 10 Binding to Hair (Quantitative) In order to be able to demonstrate the binding strength of KBD to hair also relative to other proteins, a quantitative assay was developed (see also FIG. 7). In this test, hair was firstly incubated with KBD and excess KBD was washed off. An antibody-peroxidase conjugate was then coupled via the His tag of the KBD. Nonbound antibody peroxidase conjugate was washed off again. The bound antibody-peroxidase conjugate Monoclonal AntipolyHisti dine Peroxidase Conjugate, produced in mouse, lyophilized powder, Sigma can convert a colorless substrate (TMB) into a colored product, which can be measured photometri cally at 405 nm. The intensity of the absorption indicates the amount of bound KBD or comparison protein. The com parison protein chosen was, for example, YaaD from B.

51 US 2008/ A1 Mar. 27, 2008 subtilis, which likewise had as is necessary for this test a His tag for the detection. Instead of the His tag, other specific antibodies conjugated with peroxidase can also be used. 5 mg of hair (human) are cut into sections 5 mm in length and transferred to Eppendorf vessels (protein low-bind) in order to carry out the binding demonstration: 0375 Addition of 1 ml of ethanol for degreasing 0376 Centrifugation, removal of ethanol and washing of the hair with HO 0377 Addition of 1 ml of 1% BSA in PBS and incubation for 1 h at room temperature, gentle Swirling movements Centrifugation, removal of the supernatant 0379 Addition of the keratin-binding domains to be tested (coupled to tag e.g. His HA etc.) or control protein in 1 ml of PBS/0.05% Tween 20; incubation for 16 h at 4 C. (or at least 2 hat room temperature) with gentle Swimming movements Centrifugation, removal of the supernatant (0381 3x washing with PBS/0.05% Tween Incubation with 1 ml monoclonal mouse anti-tag (His6 or HA) antibodies with peroxidase conjugate (1:2000 in PBS/0.05% Tween 20) Monoclonal Anti polyhistidine Peroxidase Conjugate, produced in mouse, lyophilized powder, Sigma for 2-4 h at room temperature, gentle Swinging movement (0383 3x washing with PBS/0.05% Tween Addition of peroxidase substrate (1 ml/eppen dorf vessel) 0385 Allow reaction to proceed until blue coloration (about 2 minutes). (0386 Stop the reaction with 100 ul of 2 MHSO The absorption is measured at 405 nm. Peroxidase Substrate (Prepare Shortly Beforehand): ml TMB solution (42 mm TMB in DMSO) +10 ml of substrate buffer (0.1 M sodium acetate ph 4.9) ul H2O 3% strength BSA=Bovine serum albumin PBS=Phosphate buffered salt solution Tween 20 polyoxyethylene sorbitan monolaurate, n about 2O TMB-3.5.3',5'-tetramethylbenzidine A binding test on hair carried out by way of example for KBD-B demonstrated considerable superiority of the binding of KBD-B to hair compared with significantly poorer binding of the comparison protein YaaD: TABLE 1. Quantitative KBD activity test Hair: 1 Buffer A405 n = Comparison protein YaaD Aaos = KBD-B denatured Aaos = KBD-B renatured A405 n = buffer: 2 comparison protein YaaD; 3 KBD-B denatured: 4 KBD-B renatured. The table shows the measured absorption values at 405 nm. EXAMPLE 1 OA Coupling of a Dye to KBD-B In order to couple a fluorescent dye (Alexa Fluor 532, Molecular Probes/Invitrogen) to the KBD-B protein, the dye was coupled via a maleic acid diimide linker to a cysteine thiol group by the following protocol. The reaction is depicted in FIG ) 1 mg of Alexa Fluor 532 was dissolved in 150 ul of PBS buffer of ph 7.0; this was followed by brief centrifugation to remove any undissolved constituents 0392) 10 ul of dissolved dye were added to 100 ug of KBD-B (1 mg/ml) The mixture was incubated covered with Al foil, on a shaker at 450 pm and at 24 C. for 1 hour ul of 1MDTT were added to inactivate the maleic acid diimide function of unreacted Alexa Fluor Incubation was then carried out at 450 pm and at 24 C. (covered with Al foil) for 30 minutes 0396 Coupling of KBD-B with coupled Alexa Fluor 532 to skin/hair can be determined by an activity test (see example 9 and 10). The KBD-B-Alexa Fluor 532 coupling which is bound to skin or hair in analogy to example 9 or 10 can be detected very easily on hair under the fluorescence microscope (detection with absorption: 532 nm/emission: 590 nm, see FIG. 9) or with the naked eye on bleached hair. All 1%: 0397) EXAMPLE 11 Use of the KBD in an Emulsion for Daycare O/W Type.7 Ceteareth-6, Stearyl Alcohol 0.7 Ceteareth Diethylamino Hydroxybenzoyl Hexyl Benzoate 2.0 PEG-14 Dimethicone 3.6 Cetearyl Alcohol 6.0 Ethylhexyl Methoxycinnamate 2.0 Dibutyl Adipate Glycerin 0.2 Disodium EDTA 1.0 Panthenol q.s. Preservative 67.8 Aqua dem. Caprylic Capric Triglyceride, Sodium Acrylates Copolymer Sodium Ascorbyl Phosphate 1.0 Tocopheryl Acetate 0.2 Bisabolol 1.0 Caprylic Capric Triglyceride, Sodium Ascorbate, Tocopherol, Retinol 1.0 Aqueous solution with about 5% keratin-binding domain active ingredient Sodium Hydroxide

52 US 2008/ A1 24 Mar. 27, 2008 A1 5%: 0398 A. 1.7 Ceteareth-6, Stearyl Alcohol 0.7 Ceteareth Diethylamino Hydroxybenzoyl Hexyl Benzoate 2.0 PEG-14 Dimethicone 3.6 Cetearyl Alcohol 6.0 Ethylhexyl Methoxycinnamate 2.0 Dibutyl Adipate B 5.0 Glycerin 0.2 Disodium EDTA 1.0 Panthenol q.s. Preservative 63.8 Aqua dem. C 4.0 Caprylic? Capric Triglyceride, Sodium Acrylates Copolymer D 0.2 Sodium Ascorbyl Phosphate 1.0 Tocopheryl Acetate 0.2 Bisabolol 1.0 Caprylic Capric Triglyceride, Sodium Ascorbate, Tocopherol, Retinol 5.0 Aqueous solution with about 5% keratin-binding domain active ingredient Sodium Hydroxide Preparation: Heat phases A and B separately from one another to about 80 C. Stir Phase B into phase A and homogenize. Stir phase C into the combined phases A and B and homogenize again. Cool with stirring to about 40 C. add phase D, adjust the ph to about 6.5 using phase E. homogenize and cool to room temperature with stirring. Note: The formulation is prepared without protective gas. Bottling must take place into oxygen-impermeable packag ings, e.g. aluminum tubes. All 1%: 0399 EXAMPLE 12 Use of the KBD in a protective day cream O/W type A. 1.7 Ceteareth-6, Stearyl Alcohol 0.7 Ceteareth Diethylamino Hydroxybenzoyl Hexyl Benzoate 2.0 PEG-14 Dimethicone 3.6 Cetearyl Alcohol 6.0 Ethylhexyl Methoxycinnamate 2.0 Dibutyl Adipate B 5.0 Glycerin 0.2 Disodium EDTA 1.0 Panthenol q.s. Preservative 68.6 Aqua dem. C 4.0 Caprylic? Capric Triglyceride, Sodium Acrylates Copolymer D 1.0 Sodium Ascorbyl Phosphate 1.0 Tocopheryl Acetate 0.2 Bisabolol -continued 1.0 Aqueous solution with about 5% keratin-binding domain active ingredient E q.s. Sodium Hydroxide A1 5%: A. 1.7 Ceteareth-6, Stearyl Alcohol 0.7 Ceteareth Diethylamino Hydroxybenzoyl Hexyl Benzoate 2.0 PEG-14 Dimethicone 3.6 Cetearyl Alcohol 6.0 Ethylhexyl Methoxycinnamate 2.0 Dibutyl Adipate B 5.0 Glycerin 0.2 Disodium EDTA 1.0 Panthenol q.s. Preservative 64.6 Aqua dem. C 4.0 Caprylic? Capric Triglyceride, Sodium Acrylates Copolymer D 1.0 Sodium Ascorbyl Phosphate 1.0 Tocopheryl Acetate 0.2 Bisabolol 5.0 Aqueous solution with about 5% keratin-binding domain active ingredient E q.s. Sodium Hydroxide Preparation: Heat phases A and B separately from one another to about 80 C. Stir phase B into phase A and homogenize. Incorporate phase C into the combined phases A and B and homogenize. Cool with stirring to about 40 C. Add phase D, adjust the ph to about 6.5 using phase E and homogenize. Cool to room temperature with stirring. EXAMPLE 13 Use of the KBD in a face-cleansing lotion O/W type All 1%: A 10.0 Cetearyl Ethylhexanoate 10.0 Caprylic/Capric Triglyceride 1.5 Cyclopentasiloxane, Cyclohexasiloxane 2.0 PEG-40 Hydrogenated Castor Oil B 3.5 Caprylic? Capric Triglyceride, Sodium Acrylates Copolymer C 1.0 Tocopheryl Acetate 0.2 Bisabolol q.s. Preservative q.s. Perfume oil D 3.0 Polyguaternium Cocotrimonium Methosulfate 0.5 Ceteareth Panthenol, Propylene Glycol 4.0 Propylene Glycol 0.1 Disodium EDTA 1.0 Aqueous solution with about 5% keratin-binding domain active ingredient 60.7 Aqua dem.

53 US 2008/ A1 25 Mar. 27, 2008 A1 5%: 0402 A O.O O C.S. C.S. 3.0 O.S O.S O.1 S.O Cetearyl Ethylhexanoate Caprylic Capric Triglyceride Cyclopentasiloxane, Cyclohexasiloxane PEG-40 Hydrogenated Castor Oil Caprylic Capric Triglyceride, Sodium Acrylates Copolymer Tocopheryl Acetate Bisabolol Preservative Perfume oil Polyduaternium-44 Cocotrimonium Methosulfate Ceteareth-25 Panthenol, Propylene Glycol Propylene Glycol Disodium EDTA Aqueous solution with about 5% keratin-binding domain active ingredient 56.7 Aqua dem. Preparation: Dissolve phase A. Stir phase B into phase A. Incorporate phase C into the combined phases A and B. Dissolve phase D, stir into the combined phases A, B and C and homogenize. After-stir for 15 min. All 1%: 0403 EXAMPLE 1.4 Use of the KBD in a Daily Care Body Spray A. 3.0 Ethylhexyl Methoxycinnamate 2.0 Diethylamino Hydroxybenzoyl Hexyl Benzoate 1.0 Polyguaternium Propylene Glycol 2.0 Panthenol, Propylene Glycol 1.0 Cyclopentasiloxane, Cyclohexasiloxane 10.0 Octyldodecanol 0.5 PVP 10.0 Caprylic? Capric Triglyceride 3.0 C12-15 Alkyl Benzoate 3.0 Glycerin 1.0 Tocopheryl Acetate 0.3 Bisabolol 1.0 Aqueous solution with about 5% keratin-binding domain active ingredient 59.2 Alcohol A1 5%: A. 3.0 Ethylhexyl Methoxycinnamate 2.0 Diethylamino Hydroxybenzoyl Hexyl Benzoate -continued 1.0 Polyguaternium Propylene Glycol 2.0 Panthenol, Propylene Glycol 1.0 Cyclopentasiloxane, Cyclohexasiloxane 10.0 Octyldodecanol 0.5 PVP 10.0 Caprylic? Capric Triglyceride 3.0 C12-15 Alkyl Benzoate 3.0 Glycerin 1.0 Tocopheryl Acetate 0.3 Bisabolol 5.0 Aqueous solution with about 5% keratin-binding domain active ingredient 55.2 Alcohol Preparation: Weigh in the components of phase A and dissolve until clear. All 1%: 0405 EXAMPLE 1.5 Use of the KBD in a Skin Care Gel A. 3.6 PEG-40 Hydrogenated Castor Oil 15.0 Alcohol 0.1 Bisabolol 0.5 Tocopheryl Acetate q.s. Perfume oil B 3.0 Panthenol 0.6 Carbomer 1.0 Aqueous solution with about 5% keratin-binding domain active ingredient 75.4 Aqua dem. C 0.8 Triethanolamine A1 5%: 0406 A. 3.6 PEG-40 Hydrogenated Castor Oil 15.0 Alcohol 0.1 Bisabolol 0.5 Tocopheryl Acetate q.s. Perfume oil B 3.0 Panthenol 0.6 Carbomer 5.0 Aqueous solution with about 5% keratin-binding domain active ingredient 71.4 Aqua dem. C 0.8 Triethanolamine Preparation: Dissolve phase A until clear. Allow phase B to swell and neutralize with phase C. Stir phase A into the homogenized phase B and homogenize.

54 US 2008/ A1 Mar. 27, 2008 All 1%: 0407 EXAMPLE 16 A1 5%: Use of the KBD in an after Shave Lotion 0410 A. 0.4 Acrylates C10-30 Alkyl Acrylate Crosspolymer 15.0 Cetearyl Ethylhexanoate 0.2 Bisabolol A Cetearyl Ethylhexanoate g spher. Acetate 5.0 Tocopheryl Acetate B 4. Panthenol 1.0 Bisabolol 150 Alcohol 0.1 Perfume oil 3.0 Glycerin 0.3 Acrylates C10-30 Alkyl Acrylate Crosspolymer B 15.0 Alcohol 1.0 Panthenol 3.0 Glycerin 1.0 Aqueous solution with about 5% keratin-binding domain active ingredient 0.1 Triethanolamine 5.0 Aqueous solution with about 5% keratin-binding domain active ingredient 59.2 Aqua dem. C 0.2 Triethanolamine 63.5 Aqua dem. Preparation: Mix the components of phase A. Stir phase B into phase A with homogenization. Neutralize with phase C and homogenize again. A1 5%: EXAMPLE 1.8 All 1%: Use of the KBD in a Sunscreen Lotion A Cetearyl Ethylhexanoate 5.0 Tocopheryl Acetate Bisabolol 0.1 Perfume oil 0.3 Acrylates C10-30 Alkyl Acrylate Crosspolymer B 15.0 Alcohol Panthenol 3.0 Glycerin A. 4.5 Ethylhexyl Methoxycinnamate 5.0 Aqueous solution with about 5% keratin-binding domain 2.0 Diethylamino Hydroxybenzoyl Hexyl Benzoate active ingredient 3.0 Octocrylene 0.1 Triethanolamine 2.5 Di-C12-13 Alkyl Malate 59.5 Aqua dem. 0.5 Tocopheryl Acetate 4.0 Polyglyceryl-3 Methyl Glucose Distearate B 3.5 Cetearyl Isononanoate Preparation: Mix the components of phase A. Dissolve 1.0 VP/Eicosene Copolymer 5.0 Isohexadecane phase B, incorporate into phase A and homogenize. 2.5 Di-C12-13 Alkyl Malate EXAMPLE 17 C Titanium Dioxide, Trimethoxycaprylylsilane Glycerin Use of the KBD in an after Sun Lotion 1.0 O.S Sodi Cet Sulfat RN tary 8t All 1%: 59.7 Aqua dem. 0. D 1.0 Aqueous solution with about 5% keratin-binding domain active ingredien Phenoxyethanol, Methylparaben, Ethylparaben, Butylparaben, Propyl paraben, Isobutylparaben 0.3 Bisabolol A. 0.4 Acrylates C10-30 Alkyl Acrylate Crosspolymer 15.0 Cetearyl Ethylhexanoate A1 5%: 0.2 Bisabolol 1.0 Tocopheryl Acetate q.s. Perfume oil 0412 B 1.0 Panthenol 15.0 Alcohol 3.0 Glycerin 1.0 Aqueous solution with about 5% keratin-binding domain active ingredient 63.2 Aqua dem. A. 4.5 Ethylhexyl Methoxycinnamate C 0.2 Triethanolamine 2.0 Diethylamino Hydroxybenzoyl Hexyl Benzoate 3.0 Octocrylene

55 US 2008/ A1 27 Mar. 27, continued 2.5 Di-C12-13 Alkyl Malate 0.5 Tocopheryl Acetate 4.0 Polyglyceryl-3 Methyl Glucose Distearate B 3.5 Cetearyl Isononanoate 1.0 VP/Eicosene Copolymer 5.0 Isohexadecane 2.5 Di-C12-13 Alkyl Malate 3.0 Titanium Dioxide, Trimethoxycaprylylsilane C 5.0 Glycerin 1.0 Sodium Cetearyl Sulfate 0.5 Xanthan Gum 55.7 Aqua dem. D 5.0 Aqueous solution with about 5% keratin-binding domain active ingredien 1.0 Phenoxyethanol, Methylparaben, Ethylparaben, Butylparaben, Propyl paraben, Isobutylparaben 0.3 Bisabolol Preparation: Heat the components of phases A and B sepa rately from one another to about 80 C. Stir phase B into phase A and homogenize. Heat phase C to about 80 C. and stir into the combined phases A and B with homogenization. Cool to about 40 C. with stirring, add phase D and homogenize again. All 1%: 0413 EXAMPLE 19 Use of the KBD in a Sunscreen Lotion O/W Type A. 2.0 Ceteareth-6, Stearyl Alcohol 2.0 Ceteareth Tribehenin 2.0 Cetearyl Alcohol 2.0 Cetearyl Ethylhexanoate 5.0 Ethylhexyl Methoxycinnamate 1.0 Ethylhexyl Triazone 1.0 VP/Eicosene Copolymer 7.0 sopropyl Myristate B 5.0 Zinc Oxide, Triethoxycaprylylsilane C 0.2 Xanthan Gum 0.5 Hydroxyethyl Acrylate/Sodium Acryloyldimethyl Taurate Copolymer, Squalane, Polysorbate Disodium EDTA 5.0 Propylene Glycol 0.5 Panthenol 60.9 Aqua dem. D 1.0 Aqueous solution with about 5% keratin-binding domain active ingredient 0.5 Phenoxyethanol, Methylparaben, Butylparaben, Ethylparaben, Propyl paraben, Isopropylparaben 1.0 Tocopheryl Acetate 0.2 Bisabolol A1 5%: 0414 A B C D 2.0 Ceteareth-6, Stearyl Alcohol 2.0 Ceteareth Tribehenin 2.0 Cetearyl Alcohol 2.0 Cetearyl Ethylhexanoate 5.0 Ethylhexyl Methoxycinnamate 1.0 Ethylhexyl Triazone 1.0 VP/Eicosene Copolymer 7.0 Isopropyl Myristate 5.0 Zinc Oxide, Triethoxycaprylylsilane 0.2 Xanthan Gum 0.5 Hydroxyethyl Acrylate/Sodium Acryloyldimethyl Taurate Copolymer, Squalane, Polysorbate Disodium EDTA 5.0 Propylene Glycol 0.5 Panthenol 56.9 Aqua dem. 5.0 Aqueous solution with about 5% keratin-binding domain active ingredient 0.5 Phenoxyethanol, Methylparaben, Butylparaben, Ethylparaben, Propyl-paraben, Isopropylparaben 1.0 Tocopheryl Acetate 0.2 Bisabolol Preparation: Heat phase A to about 80 C., stir in phase B and homogenize for 3 min. Likewise heat phase C to 80 C. and stir into the combined phases A and B with homogeni zation. Cool to about 40 C., stir in phase D and homogenize aga1n. All 1%: 0415 EXAMPLE 20 Use of the KBD in a Sunscreen Lotion % ngredient (INCI) O/W Type A. 3.5 Ceteareth-6, Stearyl Alcohol 1.5 Ceteareth Ethylhexyl Methoxycinnamate 2.0 Diethylamino Hydroxybenzoyl Hexyl Benzoate 2.0 Cyclopentasiloxane, Cyclohexasiloxane 0.5 Beeswax 3.0 Cetearyl Alcohol 10.0 Caprylic/Capric Triglyceride B C Titanium Dioxide, Silica, Methicone, Alumina Glycerin 0.2 Disodium EDTA 0.3 Xanthan Gum 1.0 Decyl Glucoside 2.0 Panthenol, Propylene Glycol 56.3 Aqua dem. D 1.0 Aqueous solution with about 5% keratin-binding domain active ingredient 1.0 Tocopheryl Acetate 0.2 Bisabolol q.s. q.s. Perfume oil Preservative

56 US 2008/ A1 28 Mar. 27, 2008 A1 5%: 0416 % ngredient (INCI) A. 3.5 Ceteareth-6, Stearyl Alcohol 1.5 Ceteareth Ethylhexyl Methoxycinnamate 2.0 Diethylamino Hydroxybenzoyl Hexyl Benzoate 2.0 Cyclopentasiloxane, Cyclohexasiloxane O.S Beeswax Cetearyl Alcohol Caprylic Capric Triglyceride B C Titanium Dioxide, Silica, Methicone, Alumina Glycerin O.2 Disodium EDTA 0.3 Xanthan Gum D 1.O Decyl Glucoside 2.0 Panthenol, Propylene Glycol 52.3 Aqua dem. 5.0 Aqueous solution with about 5% keratin-binding domain active ingredient 1.0 Tocopheryl Acetate 0.2 Bisabolol C.S. Perfume oil C.S. Preservative Preparation: Heat phase A to about 80 C., stir in phase B and homogenize for 3 min. Likewise heat phase C to 80 C. and stir into the combined phases A and B with homogeni zation. Cool to about 40 C., stir in phase D and homogenize again. All 1%: 0417 A1 5%: 0418 EXAMPLE 21 Use of the KBD in a Foot Balsam % A S.O S.O O.2 O.S B 69.3 C.S. C 1.O 1.O D 1.O S.O % A Ingredient (INCI) Ceteareth-6, Stearyl Alcohol Ceteareth-25 Cetearyl Ethylhexanoate Cetyl Alcohol Glyceryl Stearate Mineral Oil Menthol Camphor Aqua dem. Preservative Bisabolol Tocopheryl Acetate Aqueous solution with about 5% keratin-binding domain active ingredient Witch Hazel Extract Ingredient (INCI) Ceteareth-6, Stearyl Alcohol Ceteareth-25 % -continued Ingredient (INCI) S.O Cetearyl Ethylhexanoate Cetyl Alcohol Glyceryl Stearate S.O Mineral Oil O.2 Menthol O.S Camphor B 65.3 Aqua dem. C.S. Preservative C 1.O Bisabolol D 1.O Tocopheryl Acetate S.O Aqueous solution with about 5% keratin-binding domain active ingredient S.O Witch Hazel Extract Preparation: Heat the components of phases A and B sepa rately from one another to about 80 C. Stir phase B into phase A with homogenization. Cool to about 40 C. with stirring, add phases C and D and briefly after-homogenize. Cool to room temperature with stirring. EXAMPLE 22 Use of the KBD in a W/O Emulsion with Bisabolol All 1%: 0419 A1 5%: 0420 A. 6.0 PEG-7 Hydrogenated Castor Oil 8.0 Cetearyl Ethylhexanoate 5.0 Isopropyl Myristate 15.0 Mineral Oil 0.3 Magnesium Stearate 0.3 Aluminum Stearate 2.0 PEG-45/Dodecyl Glycol Copolymer B 5.0 Glycerin 0.7 Magnesium Sulfate 55.6 Aqua dem. C 1.0 Aqueous solution with about 5% keratin-binding domain active ingredient 0.5 Tocopheryl Acetate 0.6 Bisabolol A. 6.0 PEG-7 Hydrogenated Castor Oil 8.0 Cetearyl Ethylhexanoate 5.0 Isopropyl Myristate 15.0 Mineral Oil 0.3 Magnesium Stearate 0.3 Aluminum Stearate 2.0 PEG-45/Dodecyl Glycol Copolymer B 5.0 Glycerin 0.7 Magnesium Sulfate 51.6 Aqua dem. C 5.0 Aqueous solution with about 5% keratin-binding domain active ingredient 0.5 Tocopheryl Acetate

57 US 2008/ A1 29 Mar. 27, 2008 Preparation: Heat phases A and B separately from one another to about 85 C. Stir phase B into phase A and homogenize. Cool to about 40 C. with stirring, add phase C and briefly homogenize again. Cool to room temperature with stirring. List of formulations for patent keratin-binding domain haircare All 1% 0421 A1 5% 0422 EXAMPLE 23 Foam Conditioner with Setting Agent A PVP/VA Copolymer 0.2 Hydroxyethyl Cetyldimonium Phosphate 0.2 Ceteareth Dimethicone Copolyol C.S. Perfume oil 10.0 Alcohol 1.0 Aqueous solution with about 5% keratin-binding domain active ingredient 68.1 Aqua dem Propane/Butane A PVP/VA Copolymer 0.2 Hydroxyethyl Cetyldimonium Phosphate 0.2 Ceteareth Dimethicone Copolyol C.S. Perfume oil 10.0 Alcohol 5.0 Aqueous solution with about 5% keratin-binding domain active ingredient 64.1 Aqua dem Propane/Butane Preparation: Weigh the components of phase A together, stir until everything has dissolved and bottle. All 1% 0423 EXAMPLE 24 Foam Conditioner A. 1.O Polyduaternium-4 O.S Hydroxyethyl Cetyldimonium Phosphate 1.O Aqueous solution with about 5% keratin-binding domain active ingredient C.S. Perfume oil A1 5% continued C.S. Preservative 91.5 Aqua dem. 6.O Propane/Butane A. 1.O Polyduaternium-4 O.S Hydroxyethyl Cetyldimonium Phosphate S.O Aqueous solution with about 5% keratin-binding domain active ingredient C.S. Perfume oil C.S. Preservative 87.5 Aqua dem. 6.O Propane/Butane Preparation: Weigh the components of phase A together, stir until everything has dissolved to give a clear Solution and bottle. All 1% 0425 A1 5% 0426 EXAMPLE 25 Foam Conditioner A. 1.O Polyduaternium-11 O.S Hydroxyethyl Cetyldimonium Phosphate 1.O Aqueous solution with about 5% keratin-binding domain active ingredient C.S. Perfume oil C.S. Preservative 91.5 Aqua dem. 6.O Propane/Butane A. 1.O Polyduaternium-11 O.S Hydroxyethyl Cetyldimonium Phosphate S.O Aqueous solution with about 5% keratin-binding domain active ingredient C.S. Perfume oil C.S. Preservative 87.5 Aqua dem. 6.O Propane/Butane Preparation: Weigh the components of phase A together, stir until everything has dissolved to give a clear Solution and bottle.

58 US 2008/ A1 30 Mar. 27, 2008 All 1% 0427 EXAMPLE 26 Styling Foam % Ingredient (INCI) PEG-2S PABA Hydroxyethylcellulose HFC 152 A -continued A1 5% 0428 A. 0.5 Laureth-4 C.S. Perfume oil B 77.3 Aqua dem Polyguaternium Aqueous solution with about 5% keratin-binding domain active ingredient 0.5 Dimethicone Copolyol 0.2 Ceteareth Panthenol O.1 PEG-2S PABA 0.2 Hydroxyethylcellulose C 1O.O HFC 152A A. 0.5 Laureth-4 C.S. Perfume oil B 73.3 Aqua dem Polyguaternium Aqueous solution with about 5% keratin-binding domain active ingredient 0.5 Dimethicone Copolyol 0.2 Ceteareth Panthenol O.1 PEG-2S PABA 0.2 Hydroxyethylcellulose C 1O.O HFC 152A Preparation: Mix the components of phase A. Add the components of phase B one after the other and dissolve. Bottle with phase C. All 1% 0429 EXAMPLE 27 Styling Foam A. 2.0 Cocotrimonium Methosulfate B q.s. Perfume oil 78.5 Aqua dem. 6.7 Acrylates Copolymer O.6 AMP 1.0 Aqueous solution with about 5% keratin-binding domain active ingredient 0.5 Dimethicone Copolyol 0.2 Ceteareth Panthenol A. 2.0 C.S. B O6 S.O Ingredient (INCI) Cocotrimonium Methosulfate Perfume oil Aqua dem. Acrylates Copolymer AMP Aqueous solution with about 5% keratin-binding domain active ingredient Dimethicone Copolyol Ceteareth-25 Panthenol PEG-2S PABA Hydroxyethylcellulose HFC 152 A Preparation: Mix the components of phase A. Add the components of phase B one after the other and dissolve. Bottle with phase C. All 1% 0430 EXAMPLE 28 Styling Foam A. 2.0 Cocotrimonium Methosulfate B C A1 5% 0431 q.s. Perfume oil 7.70 Polyguaternium Aqueous solution with about 5% keratin-binding domain active ingredient q.s. Preservative 79.3 Aqua dem Propane/Butane A. 2.0 Cocotrimonium Methosulfate B C q.s. Perfume oil 7.70 Polyguaternium Aqueous solution with about 5% keratin-binding domain active ingredient q.s. Preservative 75.3 Aqua dem Propane/Butane Preparation: Mix the components of phase A. Dissolve the components of phase B until clear, then stir phase B into phase A. Adjust the ph to 6-7, bottle with phase C.

59 US 2008/ A1 31 Mar. 27, 2008 All 1% 0432 EXAMPLE 29 Styling Foam A Cocotrimonium Methosulfate B C D A1 5% 0433 q.s. Perfume oil Aqua dem VP/Acrylates/Lauryl Methacrylate Copolymer O.S3 AMP 1.00 Aqueous solution with about 5% keratin-binding domain active ingredient 0.20 Ceteareth Panthenol 0.05 Benzophenone Amodimethicone, Cetrimonium Chloride, Trideceth Alcohol 0.20 Hydroxyethylcellulose 6.00 Propane/Butane A Cocotrimonium Methosulfate B C D q.s. Perfume oil Aqua dem VP/Acrylates/Lauryl Methacrylate Copolymer O.S3 AMP 5.00 Aqueous solution with about 5% keratin-binding domain active ingredient 0.20 Ceteareth Panthenol 0.05 Benzophenone Amodimethicone, Cetrimonium Chloride, Trideceth Alcohol 0.20 Hydroxyethylcellulose 6.00 Propane/Butane Preparation: Mix the components of phase A. Add the components of phase B one after the other and dissolve. Dissolve phase C in the mixture of A and B, then adjust the ph to 6-7. Bottle with phase D. All 1% 0434 A Cetrimonium Chloride B EXAMPLE 30 Styling Foam q.s. Perfume oil Aqua dem Polyguaternium Aqueous solution with about 5% keratin-binding domain active ingredient 0.20 Ceteareth Panthenol C D A1 5% continued 0.05 Benzophenone Amodimethicone, Cetrimonium Chloride, Trideceth Alcohol 0.20 Hydroxyethylcellulose 6.00 Propane/Butane A Cetrimonium Chloride B C D q.s. Perfume oil Aqua dem Polyguaternium Aqueous solution with about 5% keratin-binding domain active ingredient 0.20 Ceteareth Panthenol 0.05 Benzophenone Amodimethicone, Cetrimonium Chloride, Trideceth Alcohol 0.20 Hydroxyethylcellulose 6.00 Propane/Butane Preparation: Mix the components of phase A. Add the components of phase B one after the other and dissolve. Dissolve phase C in the mixture of A and B, then adjust the ph to 6-7. Bottle with phase D. All 1% 0436 EXAMPLE 31 Styling Foam A. q.s. PEG-40 Hydrogenated Castor Oil q.s. Perfume oil 85.5 Aqua dem. B 7.0 Sodium Polystyrene Sulfonate 1.0 Aqueous solution with about 5% keratin-binding domain active ingredient 0.5 Cetrimonium Bromide q.s. Preservative C 6.0 Propane/Butane Styling Foam A1 5% 0437 A. q.s. PEG-40 Hydrogenated Castor Oil q.s. Perfume oil 81.5 Aqua dem.

60 US 2008/ A1 32 Mar. 27, continued B 7.0 Sodium Polystyrene Sulfonate 5.0 Aqueous solution with about 5% keratin-binding domain active ingredient 0.5 Cetrimonium Bromide q.s. Preservative C 6.0 Propane/Butane Preparation: Solubilize phase A. Weigh phase B into phase A and dissolve until clear. Adjust the ph to 6-7, bottle with phase C. All 1% 0438 EXAMPLE 32 Styling Foam All 1% 0440 EXAMPLE 32 Styling Foam A. q.s. PEG-40 Hydrogenated Castor Oil q.s. Perfume oil 82.5 Aqua dem. B 10.0 Polyguaternium Aqueous solution with about 5% keratin-binding domain active ingredient 0.5 Hydroxyethyl Cetyldimonium Phosphate q.s. Preservative C 6.0 Propane/Butane A1 5% 0441 A. q.s. PEG-40 Hydrogenated Castor Oil q.s. Perfume oil 92.0 Aqua dem. B 0.5 Polyguaternium Aqueous solution with about 5% keratin-binding domain active ingredient 0.5 Cetrimonium Bromide q.s. Preservative C 6.0 Propane/Butane A1 5% 0439 A. q.s. PEG-40 Hydrogenated Castor Oil q.s. Perfume oil 88.0 Aqua dem. B 0.5 Polyguaternium Aqueous solution with about 5% keratin-binding domain active ingredient 0.5 Cetrimonium Bromide q.s. Preservative C 6.0 Propane/Butane Preparation: Solubilize phase A. Weigh phase B into phase A and dissolve until clear. Adjust the ph to 6-7, bottle with phase C. A. q.s. PEG-40 Hydrogenated Castor Oil q.s. Perfume oil 78.5 Aqua dem. B 10.0 Polyguaternium Aqueous solution with about 5% keratin-binding domain active ingredient 0.5 Hydroxyethyl Cetyldimonium Phosphate q.s. Preservative C 6.0 Propane/Butane Preparation: Solubilize phase A. Weigh phase B into phase A and dissolve until clear. Adjust the ph to 6-7, bottle with phase C. All 1% 0442 EXAMPLE 33 Styling Foam A. 2.0 Cocotrimonium Methosulfate B C q.s. Perfume oil 84.0 Aqua dem. 2.0 Chitosan 1.0 Aqueous solution with about 5% keratin-binding domain active ingredient 0.5 Dimethicone Copolyol 0.2 Ceteareth Panthenol O.1 PEG-2S PABA 1.O.O HFC 152 A

61 US 2008/ A1 Mar. 27, 2008 A1 5% 0443 A. 2.0 Cocotrimonium Methosulfate C.S. Perfume oil B 80.0 Aqua dem. 2.0 Chitosan 5.0 Aqueous solution with about 5% keratin-binding domain active ingredient 0.5 Dimethicone Copolyol 0.2 Ceteareth Panthenol O.1 PEG-2S PABA C 1O.O HFC 152A Preparation: Mix the components of phase A. Add the components of phase B one after the other and dissolve. Bottle with phase C. All 1% 0444 A1 5% 0445 EXAMPLE 34 Care Shampoo A Sodium Laureth Sulfate 6.0 Sodium Cocoamphoacetate 6.0 Cocamidopropyl Betaine 3.0 Sodium Laureth Sulfate, Glycol Distearate, Cocamide MEA, Laureth Aqueous solution with about 5% keratin-binding domain active ingredient 7.7 Polyguaternium Amodimethicone C.S. Perfume oil C.S. Preservative 1.0 Sodium Chloride 43.3 Aqua dem. B C.S. Citric Acid Preparation: Mix the components of phase A and dissolve. Adjust the ph to 6-7 with citric acid. All 1% 0446 A1 5% 0447 EXAMPLE 35 Shower Gel A Sodium Laureth Sulfate 5.0 Decyl Glucoside 5.0 Cocamidopropyl Betaine 1.0 Aqueous solution with about 5% keratin-binding domain active ingredient 1.0 Panthenol C.S. Perfume oil C.S. Preservative 2.0 Sodium Chloride 46.0 Aqua dem. B C.S. Citric Acid A Sodium Laureth Sulfate 5.0 Decyl Glucoside 5.0 Cocamidopropyl Betaine 5.0 Aqueous solution with about 5% keratin-binding domain active ingredient 1.0 Panthenol C.S. Perfume oil C.S. Preservative 2.0 Sodium Chloride 42.0 Aqua dem. B C.S. Citric Acid Preparation: Mix the components of phase A and dissolve. Adjust the ph to 6-7 with citric acid. All 1% 0448 EXAMPLE 36 Shampoo A Sodium Laureth Sulfate 6.0 Sodium Cocoamphoacetate 6.0 Cocamidopropyl Betaine 3.0 Sodium Laureth Sulfate, Glycol Distearate, Cocamide MEA, Laureth Aqueous solution with about 5% keratin-binding domain active ingredient 7.7 Polyguaternium Amodimethicone C.S. Perfume oil C.S. Preservative 1.0 Sodium Chloride 39.3 Aqua dem. B C.S. Citric Acid % A. 40.O S.O C.S O O.3 1.O C.S. 1.O 2.0 Ingredient (INCI) Sodium Laureth Sulfate Sodium C12-15 Pareth-15 Sulfonate Decyl Glucoside Perfume oil Phytantriol Aqua dem. Aqueous solution with about 5% keratin-binding domain active ingredient Polyguaternium-10 Panthenol Preservative Laureth-3 Sodium Chloride

62 US 2008/ A1 34 Mar. 27, 2008 A1 5% 0449) A Sodium Laureth Sulfate 5.0 Sodium C12-15 Pareth-15 Sulfonate 5.0 Decyl Glucoside C.S. Perfume oil 0.1 Phytantriol 40.6 Aqua dem. 5.0 Aqueous solution with about 5% keratin-binding domain active ingredient 0.3 Polyguaternium Panthenol C.S. Preservative 1.0 Laureth Sodium Chloride Preparation: Mix the components of phase A and dissolve. Adjust the ph to 6-7 with citric acid. All 1% 0450 A1 5% 0451 EXAMPLE 37 Shampoo A Cocamidopropyl Betaine Disodium Cocoamphodiacetate 5.00 Polysorbate Decyl Glucoside C.S. C.S. Perfume oil Preservative 1.00 Aqueous solution with about 5% keratin-binding domain active ingredient 0.15 Guar Hydroxypropyltrimonium Chloride 2.00 Laureth Aqua dem. C.S. Citric Acid B 3.00 PEG-150 Distearate A Cocamidopropyl Betaine Disodium Cocoamphodiacetate 5.00 Polysorbate Decyl Glucoside C.S. C.S. Perfume oil Preservative 5.00 Aqueous solution with about 5% keratin-binding domain active ingredient 0.15 Guar Hydroxypropyltrimonium Chloride 2.00 Laureth-3 -continued Aqua dem. C.S. Citric Acid B 3.00 PEG-150 Distearate Preparation: Weigh in the components of phase A and dissolve. Adjust the ph to 6-7. Add phase B and heat to about 50 C. Cool to room temperature with stirring. EXAMPLE 38 Moisturizing Bodycare Cream All 1% 0452 A1 5% 0453 A. 2.0 Ceteareth Ceteareth-6, Stearyl Alcohol 3.0 Cetearyl Ethylhexanoate 1.0 Dimethicone 4.0 Cetearyl Alcohol 3.0 Glyceryl Stearate SE 5.0 Mineral Oil 4.0 Simmondsia Chinensis (Jojoba) Seed Oil 3.0 Mineral Oil, Lanolin Alcohol B 5.0 Propylene Glycol 1.0 Aqueous solution with about 5% keratin-binding domain active ingredient 1.0 Panthenol 0.5 Magnesium Aluminum Silicate C.S. Preservative 65.5 Aqua dem. C C.S. Perfume oil D C.S. Citric Acid A. 2.0 Ceteareth Ceteareth-6, Stearyl Alcohol 3.0 Cetearyl Ethylhexanoate 1.0 Dimethicone 4.0 Cetearyl Alcohol 3.0 Glyceryl Stearate SE 5.0 Mineral Oil 4.0 Simmondsia Chinensis (Jojoba) Seed Oil 3.0 Mineral Oil, Lanolin Alcohol B 5.0 Propylene Glycol 5.0 Aqueous solution with about 5% keratin-binding domain active ingredient 1.0 Panthenol 0.5 Magnesium Aluminum Silicate C.S Preservative 61.5 Aqua dem. C C.S. Perfume oil D C.S. Citric Acid Preparation: Heat phases A and B separately to about 80 C. Briefly prehomogenize phase B, then stir phase B into phase A and homogenize again. Cool to about 40 C., add phase C and homogenize thoroughly again. Adjust the ph to 6-7 with citric acid.

63 US 2008/ A1 Mar. 27, 2008 All 1% 0454) EXAMPLE 39 Moisturizing Bodycare Cream A. 6.0 PEG-7 Hydrogenated Castor Oil 10.0 Cetearyl Ethylhexanoate 5.0 Isopropyl Myristate 7.0 Mineral Oil 0.5 Shea Butter (Butyrospermum Parkii) 0.5 Aluminum Stearate 0.5 Magnesium Stearate 0.2 Bisabolol 0.7 Quaternium-18-Hectorite B 5.0 Dipropylene Glycol 0.7 Magnesium Sulfate C.S. Preservative 62.9 Aqua dem. C C.S. Perfume oil 1.0 Aqueous solution with about 5% keratin-binding domain active ingredient A. 6.0 PEG-7 Hydrogenated Castor Oil 10.0 Cetearyl Ethylhexanoate 5.0 Isopropyl Myristate 7.0 Mineral Oil 0.5 Shea Butter (Butyrospermum Parkii) 0.5 Aluminum Stearate 0.5 Magnesium Stearate 0.2 Bisabolol 0.7 Quaternium-18-Hectorite B 5.0 Dipropylene Glycol 0.7 Magnesium Sulfate C.S. Preservative 58.9 Aqua dem. C C.S. Perfume oil S.O Aqueous solution with about 5% keratin-binding domain active ingredient 0455 Preparation: Heat phases A and B separately to about 80 C. Stir phase B into phase A and homogenize. Cool to about 40 C. with stirring, add phase C and homog enize again. Allow to cool to room temperature with stirring. All 1% 0456 EXAMPLE 40 Liquid Make-Up O/W Type A. 2.0 Ceteareth-6, Stearyl Alcohol 2.0 Ceteareth-25 6.O 1.O Glyceryl Stearate Cetyl Alcohol 8.0 Mineral Oil A1 5% continued 7.0 Cetearyl Ethylhexanoate 0.2 Dimethicone B 3.0 Propylene Glycol 1.0 Panthenol C.S. Preservative 61.9 Aqua dem. C 0.1 Bisabolol 1.0 Aqueous solution with about 5% keratin-binding domain active ingredient C.S. Perfume oil C.I , Titanium Dioxide 1.1 Iron Oxides A. 2.0 Ceteareth-6, Stearyl Alcohol 2.0 Ceteareth Glyceryl Stearate 1.0 Cetyl Alcohol 8.0 Mineral Oil 7.0 Cetearyl Ethylhexanoate 0.2 Dimethicone B 3.0 Propylene Glycol 1.0 Panthenol C.S. Preservative 57.9 Aqua dem. C 0.1 Bisabolol 5.0 Aqueous solution with about 5% keratin-binding domain active ingredient C.S. Perfume oil D 5.7 C.I , Titanium Dioxide 1.1 Iron Oxides Preparation: Heat phases A and B separately to about 80 C. Stir phase B into phase A and homogenize. Cool to about 40 C. with stirring, add phases C and D and thoroughly homog enize again. Allow to cool to room temperature with stirring. EXAMPLE The active ingredient employed in the following exemplary formulations was a 5% by weight aqueous solu tion of a keratin-binding domain or of a keratin-binding effector molecule. The following data are parts by weight. Clear Shampoo 0459 Ingredients (INCI) Texapon N S.OO SO Dehyaufn PK OO S.OO S.SO Cetiol HE SO S.OO 2.30 Fragance O.10 O.10 O.10 O.10 O.10 Aqueous solution with 1.O S.O O.1 O.S 1O.O keratin-binding domain active ingredient D-Panthenol USP SO 18O Preservative O.10 O.10 O.10 O.10 O.10

64 US 2008/ A1 36 Mar. 27, continued -continued Ingredients (INCI) Emulsion 1 % by Emulsion 2 % by % by wt. vol. % by wt. vol. Citric Acid O.10 O.10 O.10 O.10 O.10 Luviguat Ultra Care 1...SO 1.OO 1...SO 1.2O 1.10 C12-15 Alkyl Benzoate 1O.OO 1S.OO Sodium Chloride 1...SO SO Cyclomethicone 4.OO Aqua dem. ad 100 ad 100 ad 100 ad 100 ad 100 Dimethicone OSO Aqueous solution with S.O 1O.O keratin-binding domain active ingredient Shampoo Octyl Isostearate S.OO Myristyl Myristate ) Ceresin Glycerin 1...SO 3.00 Filter Hydroxypropyl Starch 1.OO 3.SO Phosphate Ingredients (INCI) BHT O.O2 Texapon NSO 3S.OO 40.OO S.OO Disodium EDTA Perfume, Preservative OSO C.S. O.10 C.S. Plantacare 2000 Tego Betain L7 S.OO 1O.OO 5.50 S.OO SO 3.SO S.OO Colorant Potassium Hydroxide C.S. C.S. C.S. C.S. Fragrance O.10 O.10 O.10 O.10 O.10 Aqua dem. ad 100 ad 100 Aqueous solution with 1.O S.O O.1 O.S 1O.O adjust ph adjust ph keratin-binding domain to to O active ingredient Emulsion 1 70 VM VM D-Panthenol USP OSO 1.OO O SO O.SO Emulsion 2 35 Preservative O.10 O.10 O.10 O.10 O.10 Gas (nitrogen) 30 Citric Acid O.10 O.10 O.10 O.10 O.10 Gas (helium) Rewopal LA 3 OSO 2.OO OSO OSO Sodium Chloride 1...SO 1...SO 1...SO 1...SO 1...SO Aqua dem. ad 100 ad 100 ad 100 ad 100 ad 100 Conditioner Shampoo with Pearlescence Clear Conditioner Shampoo ) 2.OO Ingredients (INCI) Polyguaternium-10 O.SO OSO O4O Sodium Laureth Sulfate 9.OO Amphotensid GB O.OO 1S.OO 2O.OO Cocamidopropyl Betaine Plantacare 2000 S.OO 6.OO OO 4.OO Benzophenone SO OSO 1.OO Tego Betain L7 1S.OO O.OO O.OO Aqueous solution with keratin-binding 1.O S.O O.S Luviguat FC 550 O.30 O.20 O.20 O.2O O.30 domain active ingredient Fragrance O.10 O.10 O.10 O.10 O.10 Pearlescent aqueous solution with keratin- 2.OO 2.50 Aqueous solution with 2O.O S.O 1.O O.S 1O.O binding domain active ingredient keratin-binding domain Disodium EDTA O.10 O.15 O.OS active ingredient Cremophor PS 20 S.OO 1.OO OO S.OO Preservative, Perfume. Thickener Aqua dem. C.S. ad 100 C.S. ad 100 C.S. ad 100 Preservative O.10 O.10 O.10 O.10 O.10 Rewopal LA 3 2.OO 1.OO OSO 2.OO 2.00 adjust ph to 6.0 Citric Acid O.2O O.20 O.20 O.2O O.20 Stepan PEG-600 DS OO Aqua dem. ad 100 ad 100 ad 100 ad 100 ad 100 Clear Conditioner Shampoo Foam O/W Emulsions Polyguaternium-10 OSO OSO O.SO Emulsion 1 % by Emulsion 2 % by Sodium Laureth Sulfate 9.OO SO % by wt. vol. % by wt. vol. Aqueous solution with keratin-binding S.O O Stearic Acid S.OO 1.OO domain active ingredient Cetyl Alcohol 5.50 Benzophenone-3 1.OO 1...SO O.SO Cetearyl Alcohol 2.OO Imidosuccinic Acid, Na O.2O O.2O O.80 PEG-40 Stearate 8. SO Preservative, Perfume. Thickener C.S. C.S. C.S. PEG-2O Stearate 1.OO Aqua dem. ad 100 ad 100 ad 100 Caprylic Capric 4.OO 2.OO Triglyceride adjust ph to 6.0

65 US 2008/ A1 Mar. 27, Clear Conditioner Shampoo with Volume Effect -continued Bis-Ethylhexyloxyphenol 1...SO 2.OO Sodium Laureth Sulfate Ethylhexyl Methoxycinnamate 1O.OO 2.OO 10.SO 1...SO Methoxyphenyl Triazine Butyl Methoxydibenzoylmethane 2.00 Aqueous solution with keratin-binding domain active ingredient 1O.O O.1 O.S Disodium Phenyl Dibenzimidazole Tetrasulfonate 2.50 OSO 2.OO Cocamidopropyl Betaine Ethylhexyl Triazone 4.OO OO Disodium EDTA O.O1 O.10 O.O1 Octocrylene 4.OO Preservative, Perfume oil, Thickener C.S. C.S. C.S. Diethylhexyl Butamido Triazone 1.OO 2.OO Aqua dem. ad 100 ad 100 ad 100 sylbenimidazole Sulfonic OSO 3.00 Aci adjust ph to 6.0 Methylene Bis-Benzotriazolyl 2.OO OSO 1...SO Tetramethylbutylphenol Ethylhexyl Salicylate 3.00 Gel Cream Drometrizole Trisiloxane Terephthalidene Dicamphor 1...SO OSO 1.OO Sulfonic Acid 0466 Diethylhexyl 2,6-Naphthalate 3.SO 4.OO 7.OO 900 Titanium Dioxide-microfine 1.OO 3.00 Zinc Oxide-microfine O.25 Aqueous solution with keratin- O.1 O.S 1.O O.O binding domain active ingredient Cyclic Dimethylpolysiloxane S.OO 5.50 S.OO 5.50 Acrylates/C10-30 Alkylacrylate Crosspolymer O4O O.35 O4O O.35 Dimethicone Polydimethylsiloxane Glycerin 1.OO 1.OO O O O.6O 120 Polyacrylic Acid O.2O 0.22 O.2O 0.22 Sodium Hydroxide C.S. C.S. C.S. C.S. Xanthan Gum O.10 O.13 O.10 O.13 Preservative O.30 O.23 O.30 O.23 Cetearyl Alcohol Perfume O.2O O.20 C12-15 Alkyl Benzoate 4.OO 4SO 4.OO 4...SO Aqua dem. ad 100 ad 100 ad 100 ad 100 Caprylic Capric Triglyceride Uwinul A Plus TM OO 3.SO O.7S 3.SO 1.OO adjust ph to 6.0 UvaSorb K2A 3.00 Ethylhexyl Methoxycinnamate OO OW Sunscreen Formulation Glyceryl Monostearate SE OSO 1.OO SO Glyceri Stearate Citrate OO OO Stearic Acid PEG-40 Stearate OSO 2.00 Cetyl Phosphate 1.00 Sodium Cetearyl Sulfate 0.75 Stearyl Alcohol O.6O Cetyl Alcohol SO O.6O 2.OO Aqueous solution with keratin- 1O.O O.S 3.0 S.O O.1 O.O2 7.5 binding domain active ingredien Uwinul A Plus TM SO SO S.OO UWASorb K2A Ethylhexyl Methoxycinnamate S.OO 6.OO 8.OO Bis-Ethylhexyloxyphenol 1...SO Methoxyphenyl Triazine Butyl 2.OO 2.OO 1...SO Methoxydibenzoylmethane Disodium Phenyl 2.50 O.SO 2.00 O.30 Dibenzimidazole Tetrasulfonate Ethylhexyl Triazone 4.OO OO 2.00 Octocrylene 4.OO 7.50 Diethylhexyl Butamido Triazone OO 1.OO Phenylbenzimidazole Sulfonic OSO 3.00 Acid Methylene Bis-Benzotriazolyl 2.00 O.SO 1...SO 2.50 Tetramethylbutylphenol Ethylhexyl Salicylate 3.00 S.OO Drometrizole Trisiloxane O.SO 1.00 Terephthalidene Dicamphor 1...SO OO OSO Sulfonic Acid Diethylhexyl 2,6-Naphthalate 3.SO 7.OO 6.OO 9.00

66 US 2008/ A1 Mar. 27, continued Titanium Dioxide-microfine 1.OO SO 1...SO Zinc Oxide-microfine O.25 2.OO C12-15 Alkyl Benzoate O.25 4.OO 7.OO Dicaprylyl Ether 3.SO 2.00 Butylene Glycol S.OO 6.OO Dicaprylate/Dicaprate Cocoglyceride 6.OO 2.00 Dimethicone OSO 1.OO 2.00 Cyclomethicone 2.OO OSO O.SO Shea Butter 2.00 PVP Hexadecene Copolymer O.2O OSO 1.OO Glycerin S.OO 2.50 Xanthan Gum O.15 O.OS O.30 Sodium Carbomer O.20 O.15 O.2S Vitamin E Acetate O.6O O.23 O.7O 1.OO Fucogel O.OO Glycine Soya (Soybean) Oil Ethylhexyloxyglycine O.30 OSO 1...SO 1.00 DMDM Hydantaufin Glyacil-L O.60 O4O O.2O O.18 O.2O Methylparaben O.15 O.25 O.SO Phenoxyethanol 1.OO O.40 O.40 OSO O.40 Trisodium EDTA O.O2 O.OS Iminosuccinic Acid O.25 1.OO Ethanol 2.OO 1...SO O S.OO Perfume O.10 O.25 O.30 O.40 O.2O Aqua dem. ad 100 ad 100 ad 100 ad 100 ad 100 ad 100 ad 100 Hydrodispersion 0468 Ceteaereth-20 1.OO O.SO Cetyl Alcohol 1.OO Sodium Carbomer O.20 O.30 Acrylates/C10-30 Alkyl Acrylate O.SO O4O O.10 OSO Crosspolymer Xanthan Gum O.30 O.15 Aqueous solution with keratin-binding S.O O.S 3.0 O.1 1O.O domain active ingredient Uwinul A Plus TM 2.OO 1...SO UWASorb K2A 3.SO Ethylhexyl Methoxycinnamate S.OO Bis-Ethylhexyloxyphenol 1...SO Methoxyphenyl Triazine Butyl Methoxydibenzoylmethane 2.OO 2.OO Disodium Phenyl Dibenzimidazole Tetrasulfonate 2.50 OSO 2.00 Ethylhexyl Triazone 4.OO OO Octocrylene 4.OO Diethylhexyl Butamido Triazone 1.OO OO Phenylbenzimidazole Sulfonic Acid O.SO 3.00 Methylene Bis-Benzotriazolyl 2.OO OSO 1...SO 2.50 Tetramethylbutylphenol Ethylhexyl Salicylate 3.00 Drometrizole Trisiloxane OSO Terephthalidene Dicamphor Sulfonic 1...SO OO Acid Diethylhexyl 2,6-Naphthalate 7.OO 9.OO Titanium Dioxide-microfine 1.OO SO Zinc Oxide-microfine O.25 C12-15 Alkyl Benzoate 2.OO 2.50 Dicaprylyl Ether 4.OO Butylene Glycol Dicaprylate/Dicaprate 4.OO 2.OO 6.OO Dicaprylyl Carbonate OO Dimethicone OSO 1.OO

67 US 2008/ A1 Mar. 27, continued Phenyl Trimethicone 2.OO OSO Shea Butter 2.00 S.OO PVP Hexadecene Copolymer Tricontanyl PVP O.SO O.SO 1.OO O.SO 1.OO Ethylhexylglycerin 1.OO O.8O Glycerin Glycine Soya I 1...SO 1.OO Vitamin E Acetate O.SO O.25 1.OO Alpha Glucosilrutin Fucogel 1060 O OSO O.25 2.OO DMDM Hydanaufin Glyacil-S O.20 O60 O45 O.25 Methylparaben O.SO O.25 O.15 Phenoxyethanol O.SO O Trisodium EDTA O.O1 O.OS O.10 Ethanol SO 7.OO Perfume O.20 O.OS O.40 Aqua dem. ad 100 ad 100 ad 100 ad 100 ad WO Sunscreen Emulsion Cetyldimethicone Copolyol OO Polyglyceryl-2 Dipolyhydroxystearate S.OO 4...SO PEG-30 Dipolyhydroxystearate 5.00 Aqueous solution with keratin-binding S.O 1.O 1O.O O.S O.1 domain active ingredient Uwinul A Plus TM SO OO 2.10 UWASorb K2A 2.OO Ethylhexyl Methoxycinnamate S.OO Bis-Ethylhexyloxyphenol Methoxyphenyl 1...SO Triazine Butyl Methoxydibenzoylmethane OO Disodium Phenyl Dibenzimidazole Tetrasulfonate 2.50 O.SO 2.00 Ethylhexyl Triazone 4.OO OO Octocrylene 4.OO Diethylhexyl Butamido Triazone OO Phenylbenzimidazole Sulfonic Acid OSO 3.00 Methylene Bis-Benzotriazolyl 2.00 O.SO 1...SO 2.50 Tetramethylbutylphenol Ethylhexyl Salicylate 3.00 Drometrizole Trisiloxane O.SO Terephthalidene Dicamphor Sulfonic 1...SO 1.OO 1.OO Acid Diethylhexyl 2,6-Naphthalate OO Titanium Dioxide-microfine SO Zinc Oxide-microfine O.2S Mineral Oil OO C12-15 Alkyl Benzoate 9.OO Dicaprylyl Ether 1O.OO 7.OO Butylene Glycol Dicaprylate/Dicaprate OO 4.OO Dicaprylyl Carbonate S.OO 6.OO Dimethicone 4.OO 1.00 S.OO Cyclomethicone S.OO 2.OO Shea Butter 3.00 Petrolatum 4...SO PVP Hexadecene Copolymer OSO O.SO 1.OO Ethylhexylglycerin O OSO Glycerin Glycine Soya 1.OO 1...SO 1.OO MgSO 1.00 OSO O.SO MgCl O.70 Vitamin E Acetate OSO O.25 1.OO Ascorbyl Palmitate OSO 2.00 Fucogel SO 1.OO DMDM Hydanaufin O.6O O.40 O.2O

68 US 2008/ A1 Mar. 27, 2008 Methylparaben Phenoxyethanol Trisodium EDTA Ethanol Perfume Aqua dem. -continued O.SO O.25 O.1S O.SO O40 1.OO O.12 O.OS O SO O.20 O4O O.3S ad 100 ad 100 ad 100 ad 100 S.OO ad 100 Sticks continued 1 Caprylic Capric Triglyceride Octyldodecanol Butylene Glycol Dicaprylate? Dicaprate Pentaerythrityl Tetraisostearate Polyglyceryl-3 Diisostearate Bis-Diglyceryl Polyacyladipate-2 Cetearyl Alcohol Myristyl Myristate Beeswax Carnauba Wax Cera Alba C16-40 Alkyl Stearate Aqueous solution with keratin binding domain active ingredient Uwinul A Plus TM UWASorb K2A Ethylhexyl Methoxycinnamate Bis-Ethylhexyloxyphenol Methoxyphenyl Triazine Butyl Methoxydibenzoylmethane OO OO 7.OO OO O.OO 6.OO 8.OO OO 8.OO OO OO SO OO 3.00 S.OO S.OO 6.OO 6.OO 1...SO OO 1...SO O.SO OSO OSO O SO 1...SO 1...SO O.S O S.O 2.OO 1...SO OO SO OO Disodium Phenyl Dibenzimidazole Tetrasulfonate Ethylhexyl Triazone Octocrylene Diethylhexyl Butamido Triazone Phenylbenzimidazole Sulfonic Acid Methylene Bis-Benzotriazolyl Tetramethylbutylphenol Ethylhexyl Salicylate Drometrizole Trisiloxane Terephthalidene Dicamphor Sulfonic Acid Diethylhexyl 2,6-Naphthalate Titanium Dioxide-microfine Zinc Oxide-microfine Vitamin E Acetate Ascorbyl Palmitate Buxtix Chinensis Perfume, BHT Ricinus Communis Oil PIT Emulsion 0471) OO 1.OO OSO 2.OO 1.OO 0.50 O.OS 2.OO O.10 ad OO 1...SO 1.OO 1.OO O.25 ad 100 OSO OSO 3.00 OSO O.OS ad OO 4.OO 2.OO 1...SO 1.OO O.25 ad Glyceryl Monostearate SE Glyceryl Isostearate Isoceteth-20 Ceteareth-12 Ceteareth-20 PEG-1 OO Stearate Cetyl Alcohol Cetyl Palmitate Cetyl Dimethicone Copolyol Polyglyceryl-2 Aqueous solution with keratin-binding domain active ingredient Uwinul A Plus TM UWASorb K2A Ethylhexyl Methoxycinnamate Bis Ethylhexyloxyphenol Methoxyphenyl Triazine Butyl Methoxydibenzoyl methane OSO S.OO O.SO S.OO S.OO 1.OO 1.OO 2.80 S.2O 1.2O 1.OO SO O.SO 0.75 O.1 S.O O.O1 O.S 2.OO 1...SO OO 4.OO 1...SO 2.OO 2.OO 3.SO O S.OO OSO 4.OO 2.30 OSO 1.OO O SO 6.OO 1...SO 4.OO 2.OO 3.SO 3.30 OSO S.OO 1...SO 8.OO 2.50 S.OO 3.SO O SO S.OO OO

69 US 2008/ A1 Mar. 27, continued Disodium Phenyl 2.50 O.SO 2.OO O.30 Dibenzimidazole Tetrasulfonate Ethylhexyl Triazone Octocrylene 4.OO 4.OO OO 2.OO 7.50 Diethylhexyl Butamido OO OO 1.00 Triazone Phenylbenzimidazole OSO 3.00 Sulfonic Acid Methylene Bis O.SO 1...SO Benzotriazolyl Tetramethylbutylphenol Ethylhexyl Salicylate 3.00 S.OO Drometrizole O.SO 1.OO Trisiloxane Terephthalidene 1...SO 1.OO 1.00 OSO 1.00 Dicamphor Sulfonic Acid Diethylhexyl 2,6- Naphthalate Titanium Dioxide SO 1...SO 3.SO microfine Zinc Oxide-microfine O.25 2.OO C12-15 Alkyl Benzoate 3.SO 6.35 O.10 Cocoglyceride Dicaprylyl Ether 4...SO Dicaprylyl Carbonate Dibutyl Adipate OSO 7.00 O.30 Phenyl Trimethicone Cyclomethicone SO 2.OO Ethyl Galactomannan Hydrogenated Coco- Glycerides OO Abil Wax SO 2.OO PVP Hexadecene 1.OO 120 Copolymer Glycerin 4.OO 6.OO S.OO O.OO Vitamin E Acetate O.20 O.30 O.40 O.30 Shea Butter 2.OO OO Iodopropyl O.12 O.20 Butylcarbamate Fucogel 1000 O.10 DMDM Hydanaufin O.10 O.12 O.13 Methylparaben OSO O.30 O.35 Phenoxyethanol OSO O4O 1.OO Ocaufxyglycerin O O3S Ethanol S.OO Trisodium EDTA O40 O.15 O20 Perfume O.20 O.20 O.24 O16 O.10 O.10 Aqua dem. ad 100 ad 100 ad 100 ad 100 ad 100 ad 100 ad 100 ad 100 Gel Cream continued Aqueous solution with keratin- O.S 1O.O 3.0 S.O binding domain active ingredient Acrylate/C10-30 Alkyl acrylate Crosspolymer O4O O Dihydroxyaceaufn Cyclic Dimethylpolysiloxane S.OO S.OO S.OO 5.50 Polyacrylic acid O.2O O.22 O.2O O.22 Dimethicone Polydimethylsiloxane 1.OO O O.6O Luvigel EM 1...SO 2. SO Glycerin 1.OO Xanthan Gum O.10 O.13 O.10 O.13 Sodium Hydroxide C.S. C.S. C.S. C.S. Cetearyl Alcohol Preservative O.30 O.23 O.30 O.23 C12-15 Alkyl Benzoate 4.OO 4SO 4.OO 4...SO Perfume O.2O O.20 Caprylic Capric Triglyceride SO SO Aqua dem. ad 100 ad 100 ad 100 ad 100 Titanium Dioxide-microfine 1.OO 1...SO adjust ph to 6.0 Zinc Oxide-microfine 2.00 O.25

70 US 2008/ A1 Mar. 27, OW Self-Tannings Formulations Glyceryl Monostearate SE OSO 1.OO SO Glyceryl Stearate Citrate OO 4.OO Stearic Acid OO PEG-40 Stearate OSO 2.OO Cetyl Phosphate 1.OO Cetearyl Sulfate 0.75 Stearyl Alcohol OO O.60 Cetyl Alcohol SO O.60 2.OO Aqueous solution with O.1 O.S O.O2S S.O 3.0 1O.O 1.O keratin-binding domain active ingredient Dihydroxyaceaufn 3.00 S.OO 4 Titanium Dioxide SO 1...SO microfine Zinc Oxide-microfine O.25 2.OO C12-15 Alkyl Benzoate O.25 4.OO 7.OO Dicaprylyl Ether 3.SO 2.00 Butylene Glycol S.OO 6.OO Dicaprylate/Dicaprate Cocoglycerides 6.OO 2.00 Dimethicone OSO Cyclomethicone 2.00 O.SO O.SO Shea Butter 2.OO PVP Hexadecene O.20 OSO 1.OO Copolymer Glycerin S.OO 2.50 Xanthan Gum O.15 O.OS O.30 Sodium Carbomer O.2O O.15 O.25 Vitamin E Acetate O60 O.23 O.70 1.OO Fucogel Glycine Soya Ethylhexyloxyglycine O.30 OSO 1...SO 1.OO DMDM Hydanaufin Glyacil-L O.6O O.40 O.2O O.18 O.20 Methylparaben O.15 O.25 O.SO Phenoxyethanol 1.00 O4O O.40 OSO O40 Trisodium EDTA O.O2 O.OS Iminosuccinic Acid O Ethanol SO O S.OO Perfume O.10 O.25 O.30 O.40 O.2O Aqua dem. ad 100 ad 100 ad 100 ad 100 ad 100 ad 100 ad 100 OW Make Up 0474) Glyceryl Monostearate SE OSO SO Glyceri Stearate Citrate 2.OO OO 4.OO Stearic Acid OO PEG-40 Stearate OSO 2.00 Cetyl Phosphate 1.00 Cetearyl Sulfate 0.75 Stearyl Alcohol O.60 Cetyl Alcohol SO O.6O 2.00 Aqueous solution with 3.0 S.O 2.0 O.S 1.O S.O 1O.O keratin-binding domain active ingredient Titanium Oxide 1O.OO OO 9.SO Iron Oxide 2.OO 4.OO 3.00 S.OO OO 4.40 Zinc Oxide 4.OO 2.OO 3.00 C12-15 Alkyl Benzoate O.25 4.OO 7.00

71 US 2008/ A1 Mar. 27, continued Dicapryl Ether Butylene Glycol Dicaprylate/Dicaprate Cocoglycerides Dimethicone S.OO OSO Cyclomethicone 2.00 Shea Butter PVP Hexadecene O.20 Copolymer Glycerin 3.00 Xanthan Gum O.15 Sodium Carbomer Vitamin E Acetate O60 Glycine Soya Ethylhexyloxyglycine O.30 DMDM Hydanaufin Glyacil-L Methylparaben O.15 Phenoxyethanol 1.00 Trisodium EDTA O.O2 Iminosuccinic Acid Ethanol 2.00 Perfume O.10 Aqua dem. ad OO 7.50 O.2O 3.SO 6.OO 6.OO 1.00 O.SO O.OS O.23 O.6O O.40 O4O O.25 O.OS 1...SO O.25 O.30 ad 100 ad 100 OSO 7.50 O.15 OSO O ad O.SO 1.00 S.OO O.30 O.25 O SO O.20 O.SO O.40 OSO O.40 O2O ad 100 ad OO O40 S.OO ad 100 Self-Tanning Hydrodispersion Ceteaereth-20 Cetyl Alcohol Luvigel EM Acrylate/C10-30 Alkyl Acrylate Crosspolymer Xanthan Gum Aqueous solution with keratin-binding domain active ingredient Dihydroxyaceaufn Uwinul A Plus TM Titanium Dioxide-microfine Zinc Oxide-microfine C12-15 Alkyl Benzoate Dicapryl Ether Butylene Glycol Dicaprylate/Dicaprate Dicapryl Carbonate Dimethicone Phenyl Trimethicone Shea Butter PVP Hexadecene Copolymer Tricontanyl PVP Ethylhexylglycerin Glycerin Glycine Soya Vitamin E Acetate Alpha-Glucosilrutin DMDM Hydanaufin Glyacil-S Methylparaben Phenoxyethanol Trisodium EDTA Ethanol Perfume Water 1.OO O.SO 2.00 O O 2.OO 1...SO 1.OO OO OO 4.OO 2.00 OSO 2.OO 2.00 O.SO O.SO O.SO O.60 O.20 O.SO O.SO O60 O40 O.O O.20 ad 100 ad OO O.15 O.S OO 2.OO 6.OO 1.OO OSO 1.OO 1.OO 1...SO O.25 O45 O SO O.OS ad 100 O.SO O.10 OSO O.1 S.O S.OO 1.OO OO O.25 6.OO S.OO O.SO 1.OO O.8O OO 1.OO O.25 O.25 O O.10 7.OO O.40 ad 100 ad 100

72 US 2008/ A1 44 Mar. 27, 2008 After-Sun Hydrodispersion 0476 Ceteaereth-20 Cetyl Alcohol Luvigel (R) EM Acrylate/C10-30 Alkyl Acrylate Crosspolymer Xanthan Gum Aqueous solution with keratin-binding domain active ingredient C12-15 Alkyl Benzoate Dicapryl Ether Butylene Glycol Dicaprylate/Dicaprate Dicapryl Carbonate Dimethicone Phenyl Trimethicone Tricontanyl PVP Ethylhexylglycerin Glycerin Glycine Soya Vitamin E Acetate Alpha-Glucosilrutin Trisodium EDTA Ethanol Perfume Aqua dem O OO O.20 ad OO O.30 O.30 S.O OO 2.OO OSO 7.50 ad OO O.15 O.S 2.OO 6.OO 1.OO OSO 1.OO 1.OO 1...SO O.25 O.OS ad 100 OSO 2.50 O OO 7.50 O O40 ad OO OSO 1.O O.8O OO 1.OO O.10 9.OO ad 100 WO Emulsions 0477 Cetyl Dimethicone Copolyol Polyglyceryl-2 Dipolyhydroxystearate PEG-30 Dipolyhydroxystearate Aqueous solution with keratin-binding domain active ingredient Uwinul A Plus TM Titanium Dioxide-microfine Zinc Oxide-microfine Mineral Oil C12-15 Alkyl Benzoate Dicaprylyl Ether Butylene Glycol Dicaprylate/Dicaprate Dicaprylyl Carbonate Dimethicone Cyclomethicone Shea Butter Petrolatum PVP Hexadecene Copolymer Ethylhexylglycerin Glycerin Glycine Soya MgSO Vitamin E Acetate Ascorbyl Palmitate Fucogel 1000 DMDM Hydanaufin Methylparaben Phenoxyethanol Trisodium EDTA Ethanol Perfume Aqua dem. S.OO S.OO O.SO O.SO O O.20 ad SO O SO O OO OSO ad O.OO 2.OO 6.OO 1.OO OO 1...SO 1.OO O.25 O40 O SO O40 ad OO 1.00 O S.OO O.SO SO O.20 O O.30 O.35 ad SO 1.O SO 8.OO 7.OO 4.OO 2.OO 1.OO OSO OO O.70 1.OO 7.OO S.OO ad 100

73 US 2008/ A1 45 Mar. 27, 2008 Solid Stabilized Emulsion (Pickering Emulsions) Mineral Oil 16.OO Octyldodecanol S.OO Caprylic Capric Triglyceride OO C12-15 Alkyl Benzoate Butylene Glycol Dicaprylate/Dicaprate Dicaprylyl Ether 9.00 Dicaprylyl Carbonate 9.00 Hydroxyoctacosanyl HydroxyStearate O Disteardimonium Hecaufrite Cera Microcristallina + Paraffinum O.35 Liquidum Hydroxypropyl Methylcellulose O.10 Dimethicone Aqueous solution with keratin-binding 1.O O.S O.1 domain active ingredient Titanium Dioxide + Alumina + Simethicone + Aqua 3.00 Titanium Dioxide + Trimethoxycaprylylsilane OO Silica Dimethyl Sillylate 2.50 Boron Nitride 1.OO Starch/Sodium metaphosphate Polymer 2.00 Tapioca Starch O.SO Sodium Chloride S.OO SO Glycerin Trisodium EDTA OO Vitamin E Acetate S.OO Ascorbyl Palmitate Methylparaben O.60 Propylparaben Phenoxyethanol O.2O Hexamidine Diisethionate O4(O Diazolidinyl Urea Ethanol O.23 Perfume S.OO 3.00 Aqua dem. O.20 O.30 ad 100 ad 100 ad S.OO OO SO O.SO O.25 S.OO O.OS S.O 2.OO 4.OO 6.OO SO 1.OO 1.OO OO 1O.OO 1.OO O.20 O.20 O.SO O40 O.08 O.20 4.OO O.10 ad 100 ad 100 Sticks Caprylic Capric Triglyceride O.OO 6.OO Octyldodecanol 7.OO OO 3.00 Butylene Glycol Dicaprylate? Dicaprate Pentaerythrityl Tetraisostearate 1O.OO 6.OO 8.OO 7.00 Polyglyceryl-3 Diisostearate 2.50 Bis-Diglyceryl Polyacyladipate-2 9.OO O.OO 8.00 Cetearyl Alcohol 8.OO OO 7.00 Myristyl Myristate 3.SO OO 3.00 Beeswax S.OO S.OO 6.OO 6.OO Carnauba Wax 1...SO OO 1...SO -continued Cera Alba OSO O.SO OSO O4O C16-40 Alkyl Stearate 1...SO 1...SO 1...SO Aqueous solution with keratin- 1O.O 1.O 3.0 O.1 binding domain active ingredient Uwinul A Plus TM 2.OO 1...SO OO Titanium Dioxide-microfine 1.OO 3.00 Zinc Oxide-microfine 1.OO O.25 Vitamin E Acetate OSO 1.OO Ascorbyl Palmitate O.OS O.OS Buxtix Chinensis 2.OO 1.OO 1.OO Perfume, BHT O.10 O.25 O3S Ricinus Communis ad 100 ad 100 ad 100 ad 100

74 US 2008/ A1 Mar. 27, Self-Tanning PIT Emulsions Glyceryl Monostearate SE OSO 2.OO 3.00 S.OO OSO 4.OO Glyceryl Isostearate 3.SO 4.OO 2.OO Isoceteth-20 O.SO 2.00 Ceteareth-12 S.OO 1.OO 3.SO S.OO Ceteareth-20 S.OO 1.OO 3.SO PEG-1OO Stearate 2.8O Cetyt Alcohol S.2O OO 1.30 OSO O.30 Cetyl Palmitate SO OSO 1...SO Cetyl Dimethicone Copolyol OSO 1.OO Polyglyceryl O.30 Aqueous solution with O.1 O.S O.O1 S.O O.S 3.0 O.O2S 1O.O keratin-binding domain active ingredient Dihydroxyaceaufn 3.00 S.OO 4.OO Uwinul A Plus TM 2.OO 1...SO OO SO SOO 2.10 Titanium Dioxide-microfine 1.OO 1...SO 3.SO 1...SO 1.OO Zinc Oxide-microfine 1.OO O.25 2.OO 1...SO C12-15 Alkyl Benzoate 3.SO 6.35 O.10 Cocoglycerides OO Dicapryl Ether 4...SO Dicaprylyl Carbonate OO Dibutyl Adipate OSO O.30 Phenyl Trimethicone 2.OO OO Cyclomethicone 3.00 Ethyl Galacaufmannan O.SO 2.00 Hydrogenated Coco OO Glycerides Abil Wax SO 2.OO PVP Hexadecene 1.OO 120 Copolymer Glycerin 4.OO 6.OO S.OO O.OO Vitamin E Acetate O.2O O.30 O40 O.30 Shea Butter 2.OO OO Iodopropyl Butylcarbamate O.12 O.20 DMDM Hydanaufin O.10 O.12 O.13 Methylparaben O.SO O.30 O.35 Phenoxyethanol OSO O40 1.OO Ocaufxyglycerin O O3S Ethanol 2.OO 2.00 S.OO Trisodium EDTA O4O O.15 O.2O Perfume O.2O O.20 O.24 O O.10 Aqua dem. ad 100 ad 100 ad 100 ad 100 ad 100 ad 100 ad 100 ad 100 -continued Caprylic Capric Triglyceride O.OO 6.OO Propylene Carbonate 1S.OO 2O.OO Octyldodecanol Butylene Glycol 7.OO OO Aqueous solution with keratinbinding domain active ingredient 1.O O.S 3.0 S.O Dicaprylate/Dicaprate Vitamin E Acetate OSO 1.00 Pentaerythrityl Tetraisostearate 1O.OO 6.OO 8.OO 7.00 Ascorbyl Palmitate O.OS O.OS Polyglyceryl-3 Diisostearate 2.50 Buxtix Chinensis 2.OO Bis-Diglyceryl Polyacyladipate-2 9.OO O.OO 8.00 Perfume, BHT O.10 O.25 O.35 Myristyl Myristate 3.SO OO 3.00 Ricinus Communis ad 100 ad 100 ad 100 ad 100 Benaufne-34 S.OO S.OO 6.OO 6.OO

75 US 2008/ A1 Mar. 27, Oil Gel SEQUENCE LISTING <16O NUMBER OF SEO ID NOS : 16 <210 SEQ ID NO 1 <211 LENGTH: 2871 &212> TYPE: PRT <213> ORGANISM: Homo sapiens <4 OO SEQUENCE: 1 Met Ser Cys Asn Gly Gly Ser His Pro Arg Ile Asn Thr Lieu. Gly Arg O 15 Met Ile Arg Ala Glu Ser Gly Pro Asp Lieu. Arg Tyr Glu Val Thir Ser 2O 25 3O Gly Gly Gly Gly Thr Ser Arg Met Tyr Tyr Ser Arg Arg Gly Val Ile 35 4 O 45 Thr Asp Glin Asn Ser Asp Gly Tyr Cys Glin Thr Gly Thr Met Ser Arg SO 55 6 O His Glin Asn Glin Asn. Thir Ile Glin Glu Lieu. Lieu. Glin Asn. Cys Ser Asp s 8O Cys Lieu Met Arg Ala Glu Lieu. Ile Val Glin Pro Glu Lieu Lys Tyr Gly Asp Gly Ile Gln Lieu. Thr Arg Ser Arg Glu Lieu. Asp Glu. Cys Phe Ala 1OO O Glin Ala Asn Asp Gln Met Glu Ile Lieu. Asp Ser Lieu. Ile Arg Glu Met O 125 Arg Gln Met Gly Glin Pro Cys Asp Ala Tyr Glin Lys Arg Lieu. Lieu. Glin 13 O O Lieu. Glin Glu Gln Met Arg Ala Lieu. Tyr Lys Ala Ile Ser Val Pro Arg Val Arg Arg Ala Ser Ser Lys Gly Gly Gly Gly Tyr Thr Cys Glin Ser O 17s Gly Ser Gly Trp Asp Glu Phe Thr Lys His Val Thr Ser Glu. Cys Lieu. 18O O Gly Trp Met Arg Glin Glin Arg Ala Glu Met Asp Met Val Ala Trp Gly 195 2OO 2O5 Val Asp Lieu Ala Ser Val Glu Gln His Ile Asn. Ser His Arg Gly Ile 21 O O His Asn. Ser Ile Gly Asp Tyr Arg Trp Gln Lieu. Asp Llys Ile Lys Ala O O Asp Lieu. Arg Glu Lys Ser Ala Ile Tyr Glin Lieu. Glu Glu Glu Tyr Glu Asn Lieu. Lieu Lys Ala Ser Phe Glu Arg Met Asp His Lieu. Arg Glin Lieu 26 O O Glin Asn. Ile Ile Glin Ala Thir Ser Arg Glu Ile Met Trp Ile Asn Asp 27s 28O 285 Cys Glu Glu Glu Glu Lieu. Lieu. Tyr Asp Trp Ser Asp Lys Asn. Thir Asn 29 O OO Ile Ala Glin Lys Glin Glu Ala Phe Ser Ile Arg Met Ser Glin Lieu. Glu 3. OS O Val Lys Glu Lys Glu Lieu. Asn Llys Lieu Lys Glin Glu Ser Asp Gln Lieu

76 US 2008/ A1 Mar. 27, Continued Val Lieu. Asn. Glin His Pro Ala Ser Asp Llys Ile Glu Ala Tyr Met Asp 34 O O Thr Lieu Gln Thr Gln Trp Ser Trp Ile Leu Glin Ile Thr Lys Cys Ile Asp Wal His Lieu Lys Glu Asn Ala Ala Tyr Phe Glin Phe Phe Glu Glu 37 O O Ala Glin Ser Thr Glu Ala Tyr Lieu Lys Gly Lieu. Glin Asp Ser Ile Arg OO Llys Llys Tyr Pro Cys Asp Lys Asn Met Pro Lieu. Glin His Lieu. Lieu. Glu 4 OS 41O 415 Glin Ile Lys Glu Lieu. Glu Lys Glu Arg Glu Lys Ile Lieu. Glu Tyr Lys 42O O Arg Glin Val Glin Asn Lieu Val Asn Llys Ser Lys Lys Ile Val Glin Lieu O 445 Llys Pro Arg Asn. Pro Asp Tyr Arg Ser Asn Llys Pro Ile Ile Lieu. Arg Ala Lieu. Cys Asp Tyr Lys Glin Asp Gln Lys Ile Val His Lys Gly Asp s 48O Glu Cys Ile Lieu Lys Asp Asn. Asn. Glu Arg Ser Llys Trp Tyr Val Thr Gly Pro Gly Gly Val Asp Met Leu Val Pro Ser Val Gly Lieu. Ile Ile SOO O Pro Pro Pro Asn. Pro Lieu Ala Val Asp Lieu. Ser Cys Lys Ile Glu Glin O 525 Tyr Tyr Glu Ala Ile Lieu Ala Lieu. Trp Asn Gln Lieu. Tyr Ile Asn Met 53 O O Llys Ser Lieu Val Ser Trp His Tyr Cys Met Ile Asp Ile Glu Lys Ile Arg Ala Met Thir Ile Ala Lys Lieu Lys Thr Met Arg Glin Glu Asp Tyr 565 st O sts Met Lys Thir Ile Ala Asp Lieu. Glu Lieu. His Tyr Glin Glu Phe Ile Arg 58O O Asn Ser Glin Gly Ser Glu Met Phe Gly Asp Asp Asp Lys Arg Lys Ile 595 6OO 605 Gln Ser Glin Phe Thr Asp Ala Gln Lys His Tyr Glin Thr Lieu Val Ile O Gln Leu Pro Gly Tyr Pro Gln His Glin Thr Val Thr Thr Thr Glu Ile O Thr His His Gly Thr Cys Glin Asp Val Asn His Asn Llys Val Ile Glu Thir Asn Arg Glu Asn Asp Llys Glin Glu Thir Trp Met Lieu Met Glu Lieu O Glin Lys Ile Arg Arg Glin Ile Glu. His Cys Glu Gly Arg Met Thr Lieu O 685 Lys Asn Lieu Pro Lieu Ala Asp Glin Gly Ser Ser His His Ile Thr Val 69 O OO Lys Ile Asn. Glu Lieu Lys Ser Val Glin Asn Asp Ser Glin Ala Ile Ala 7 Os 71O 71s 72O Glu Val Lieu. Asn Glin Lieu Lys Asp Met Lieu Ala Asn. Phe Arg Gly Ser O 73

77 US 2008/ A1 Mar. 27, Continued Glu Lys Tyr Cys Tyr Lieu. Glin Asn. Glu Val Phe Gly Lieu. Phe Glin Lys O Lieu. Glu Asn. Ile Asn Gly Val Thr Asp Gly Tyr Lieu. Asn. Ser Lieu. Cys 7ss Thr Val Arg Ala Lieu. Lieu. Glin Ala Ile Lieu. Glin Thr Glu Asp Met Lieu O Llys Val Tyr Glu Ala Arg Lieu. Thr Glu Glu Glu Thr Val Cys Lieu. Asp 78s 79 O 79. 8OO Lieu. Asp Llys Val Glu Ala Tyr Arg Cys Gly Lieu Lys Lys Ile Lys Asn Asp Lieu. Asn Lieu Lys Llys Ser Lieu. Lieu Ala Thr Met Lys Thr Glu Lieu 82O O Gln Lys Ala Glin Glin Ile His Ser Glin Thr Ser Glin Glin Tyr Pro Leu O 845 Tyr Asp Lieu. Asp Lieu. Gly Llys Phe Gly Glu Lys Val Thr Glin Lieu. Thir Asp Arg Trp Glin Arg Ile Asp Llys Glin Ile Asp Phe Arg Lieu. Trp Asp O 87s 88O Lieu. Glu Lys Glin Ile Lys Glin Lieu. Arg Asn Tyr Arg Asp Asn Tyr Glin Ala Phe Cys Llys Trp Lieu. Tyr Asp Arg Lys Arg Arg Glin Asp Ser Lieu 9 OO O Glu Ser Met Llys Phe Gly Asp Ser Asn Thr Val Met Arg Phe Lieu. Asn O 925 Glu Gln Lys Asn Lieu. His Ser Glu Ile Ser Gly Lys Arg Asp Llys Ser 93 O O Glu Glu Val Glin Lys Ile Ala Glu Lieu. Cys Ala Asn. Ser Ile Lys Asp O Tyr Glu Lieu. Glin Lieu Ala Ser Tyr Thir Ser Gly Lieu. Glu Thir Lieu. Lieu O 97. Asn Ile Pro Ile Lys Arg Thr Met Ile Glin Ser Pro Ser Gly Val Ile 98O O Lieu. Glin Glu Ala Ala Asp Wal His Ala Arg Tyr Ile Glu Lieu. Lieu. Thr 995 1OOO 1005 Arg Ser Gly Asp Tyr Tyr Arg Phe Lieu. Ser Glu Met Lieu Lys Ser O1O O15 O2O Lieu. Glu Asp Lieu Lys Lieu Lys Asn. Thir Lys Ile Glu Val Lieu. Glu O25 O3 O O35 Glu Glu Lieu. Arg Lieu Ala Arg Asp Ala Asn. Ser Glu Asn. Cys Asn O4 O O45 OSO Lys Asn Llys Phe Lieu. Asp Glin Asn Lieu. Glin Llys Tyr Glin Ala Glu O55 O6 O O65 Cys Ser Glin Phe Lys Ala Lys Lieu Ala Ser Lieu. Glu Glu Lieu Lys Of O O7 O8O Arg Glin Ala Glu Lieu. Asp Gly Lys Ser Ala Lys Glin Asn Lieu. Asp O85 O9 O O95 Lys Cys Tyr Gly Glin Ile Lys Glu Lieu. Asn. Glu Lys 1 OO O Ile Thr Arg Lieu. Thir Tyr Glu Ile Glu Asp Glu Lys Arg Arg Arg Llys Ser Val O 125 Glu Asp Arg Phe Asp Glin Glin Lys Asn Asp Tyr Asp Gln Lieu. Glin

78 US 2008/ A1 Mar. 27, O O - Continued Lys Ala Arg Glin Cys Glu Lys Glu Asn Lieu. Gly Trp O 155 Gln Llys Lieu. Glu Ser Glu Lys Ala Ile Lys Glu Lys Glu Tyr Glu Ile Glu Arg 16 O O Lieu. Arg Val Lieu. Lieu. Glin Glu Glu Gly Thr Arg Lys Arg Glu Tyr 17s 18O 185 Glu Asn. Glu Lieu Ala Lys Val Arg Asn His Tyr Asn. Glu Glu Met OO Ser Asn Lieu. Arg Asn Llys Tyr Glu Thr Glu Ile Asn. 2O5 21 O 215 Ile Thr Lys Thir Thir Asn Lieu. Ile Lys Glu Ile Ser Met Glin Lys Glu Asp Asp Ser Lys 22O O Arg Asn Glin Lieu. Asp Arg Lieu. Ser Arg Glu Asn Arg Asp O 245 Lieu Lys Asp Glu Ile Val Arg Lieu. Asn Asp Ser Ile O Lieu. Glin Ala Thr Glu Glin Arg Arg Arg Ala Glu Glu Asn Ala Lieu O 27s Glin Gln Lys Ala Cys Gly Ser Glu Ile Met Glin Llys Lys Gln His Lieu. Glu Ile 28O O Glu Lieu Lys Glin Val Met Gln Glin Arg Ser Glu Asp ASn Ala Arg 295 3OO 305 His Lys Glin Ser Lieu. Glu Glu Ala Ala Lys Thir Ile Glin Asp Llys O Asn Lys Glu Ile Glu Arg Lieu Lys Ala Glu Phe Glin Glu Glu Ala O 335 Lys Arg Arg Trp Glu Tyr Glu Asn. Glu Lieu. Ser Llys 34 O Asn Tyr Asp Glu Glu Ile Ile Ser Lieu Lys Asn. Glin Val Arg Asn Phe Glu Thr Glu Ile Asn Ile Thr Lys Thir Thr Ile His Gln Lieu. Thr Met Gln 37O O Lys Glu Glu Asp Thir Ser Gly Tyr Arg Ala Glin Ile Asp Asn Lieu Thir Arg Glu Asn Arg Ser Lieu. Asn. Thir Ser Glu Glu Ile Lys Arg Lieu Lys 4 OO O Lieu. Thr Glin Thir Thr Glu Asn Lieu. Arg Arg Val Glu Glu O 425 Asp Ile Glin Glin Gln Lys Ala Thr Gly Ser Glu Val Ser Glin Arg 43 O O Lys Glin Gln Lieu. Glu Val Glu Lieu. Arg Glin Val Thr Gln Met Arg Thr Glu Glu Ser Val Arg Tyr Lys Glin Ser Lieu. Asp Asp Ala Ala O Llys Thir Ile Glin Asp Lys Asn Lys Glu Ile Glu Arg Lieu Lys Glin 47s 48O 485 Lieu. Ile Asp Llys Glu Thir Asn Asp Arg Lys Cys Lieu SOO Glu Asp Glu Asn Ala Arg Lieu. Glin Arg Val Glin Tyr Asp Lieu. Glin 5 OS Lys Ala Asn

79 US 2008/ A1 Mar. 27, Continued Ser Ser Ala Thr Glu Thir Ile Asn Llys Lieu Lys Val Glin Glu Glin 52O O Glu Lieu. Thir Arg Lieu. Arg Ile Asp Tyr Glu Arg Val Ser Glin Glu O 545 Arg Thr Val Lys Asp Glin Asp Ile Thr Arg Phe Glin Asn. Ser Lieu. Lys Glu Lieu. Glin Lieu Gln Lys Glin Llys Val Glu Glu Glu Lieu. Asn 565 st O sts Arg Lieu Lys Arg Thir Ala Ser Glu Asp Ser Cys Lys Arg Llys Llys 58O Lieu. Glu Glu Glu Lieu. Glu Gly Met Arg Arg Ser Lieu 595 6OO 605 Lys Glu Glin Ala Ile Lys Ile Thir Asn Lieu. Thr Glin Gln Lieu. Glu Glin Ala Ser O Ile Val Llys Lys Arg Ser Glu Asp Asp Lieu. Arg Glin Val Lieu O 635 Glin Arg Asp Asp Gly. His Lieu. Arg Glu Lys Glin Arg Thr Glin Glu Glu 64 O Lieu. Arg Arg Lieu. Ser Ser Glu Val Glu Ala Lieu. Arg Arg Glin Lieu Lieu. Glin Glu Glin Glu Ser Wall Lys Glin Ala His Lieu. Arg Asn. Glu O His Phe Gln Lys Ala Ile Glu Asp Llys Ser Arg Ser Lieu. Asn. Glu O. 695 Ser Lys Ile Glu Ile Glu Arg Lieu. Glin Ser Lieu. Thr Glu Asn Lieu. 7 OO 7Os 71O Thir Lys Glu. His Lieu Met Lieu. Glu Glu Glu Lieu. Arg Asn Lieu. Arg 71s 72 O 72 Lieu. Glu Tyr Asp Asp Lieu. Arg Arg Gly Arg Ser Glu Ala Asp Ser 73 O O Asp Lys Asn Ala Thir Ile Lieu. Glu Lieu. Arg Ser Glin Lieu. Glin Ile O 7ss Ser Asn. Asn Arg Thr Lieu. Glu Lieu. Glin Gly Lieu. Ile Asn Asp Lieu Glin Arg Glu Arg Glu Asn Lieu. Lys Glin Arg Glin Glu Ile Glu Lys Phe Glin O 78s Ala Lieu. Glu Ala Ser Asn Arg Ile Glin Glu Ser Lys Asn 79 O 79. 8OO Glin Cys Thr Glin Val Val Glin Glu Arg Glu Ser Lieu. Lieu Val Lys Ile Llys Val Lieu. Glu Glin Asp Lys Ala Arg Lieu. Glin Arg Lieu. Glu 82O O Asp Glu Lieu. Asn Arg Ala Lys Ser Thr Lieu. Glu Ala Glu Thir Arg O 845 Val Lys Glin Arg Lieu. Glu. Cys Glu Lys Glin Glin Ile Glin Asn Asp O Lieu. Asn Gln Trp Llys Thr Glin Arg Lys Tyr Ser Arg Lys Glu Glu Ala Ile O 87s Ile Glu Ser Glu Arg Glu Lys Ser Glu Arg Glu Lys Asn 88O

80 US 2008/ A1 Mar. 27, Ser Lieu. - Continued Arg Ser Glu Ile Glu Arg Lieu. Glin Ala Glu Ile Lys Arg OO 905 Ile Glu Glu Arg Cys Arg Arg Llys Lieu. Glu Asp Ser Thr Arg Glu O Thr Glin Ser Glin Lieu. Glu Thr Glu Arg Ser Arg Tyr Glin Arg Glu O 935 Ile Asp Llys Lieu. Arg Glin Arg Pro Tyr Gly Ser His Arg Glu Thr 94 O Gln Thr Glu. Cys Glu Trp Thr Val Asp Thir Ser Lys O 965 Asp Gly Lieu. Arg Llys Llys Val Thir Ala Met Gln Lieu. 97O O Lieu Val Phe Tyr Glu. Cys Glin Lieu. Ile Asp Llys Thir Thr Lieu. Asp Llys Lieu Lleu Lys Gly Lys Llys Ser Val Glu Glu Val Ala Ser Glu Ile Glin Pro Phe Lieu. Arg 2OOO Gly Ala Gly Ser Ile Ala Gly Ala Ser Ala Ser Pro Lys Glu Lys O2O 2O25 Tyr Ser Lieu Val Glu Ala Lys Arg Llys Llys Lieu. Ile Ser Pro Glu 2O3O 2O35 2O4. O Ser Thr Val Met Lieu. Lieu. Glu Ala Glin Ala Ala Thr Gly Gly Ile 2O45 2OSO 2O55 Ile Asp Pro His Arg Asn. Glu Lys Lieu. Thr Val Asp Ser Ala Ile 2O60 2O65 2. Of O Ala Arg Asp Lieu. Ile Asp Phe Asp Asp Arg Glin Glin Ile Tyr Ala Ala Glu Lys Ala Ile Thr Gly Phe Asp Asp Pro Phe Ser Gly Lys Thr Val Ser Val Ser Glu Ala Ile Llys Lys Asn Lieu. Ile Asp Arg Glu Thr Gly Met Arg Lieu. Lieu. Glu Ala Glin Ile Ala Ser Gly Gly Val Val Asp Pro Val Asn. Ser Val Phe Lieu Pro Lys Asp Val Ala Lieu Ala Arg Gly Lieu. Ile Asp Arg Asp Lieu. Tyr Arg Ser Lieu. Asn Asp Pro Arg Asp Ser Glin Lys Asn. Phe Val Asp Pro Val Thir Lys Llys Llys Val Ser Tyr Val Glin Lieu Lys Glu Arg Cys Arg Ile Glu Pro His Thr Gly Lieu. Lieu. Lieu. Lieu. Ser Val Glin Lys Arg Ser Met OO 22O5 Ser Phe Glin Gly Ile Arg Gln Pro Val Thr Val Thr Glu Lieu Val 221 O O Asp Ser Gly Ile Lieu. Arg Pro Ser Thr Val Asn. Glu Lieu. Glu Ser O 2235 Gly Glin Lieu. Glin Ile Ser Tyr Asp Glu Val Gly Glu Arg Ile Lys Asp Phe 224 O O Gly Ser Ser Cys Ile Ala Gly Ile Tyr Asn Glu Thir Thr O 2265 Lys Glin Llys Lieu. Gly Ile Tyr Glu Ala Met Lys Ile Gly Lieu Val

81 US 2008/ A1 Mar. 27, O - Continued Arg Pro Gly Thr Ala Lieu. Glu Lieu. Lieu. Glu Ala Glin O 2295 Gly Phe Ile Val Asp Pro Val Ser Asn Lieu. Arg Lieu 23 OO 23 OS 2310 Ala Ala Thr Pro Val Glu Glu Ala Tyr Lys Arg Gly Lieu Lieu. Lieu. Val Gly Ile Glu Phe Lys Glu Lys O 2325 Ser Ala Glu Arg Ala Val Thr Gly Tyr Asn Asp Pro Glu 233 O O Thr Gly Asn. Ile Ile Ser Lieu. Phe Glin Ala Met Asn Lys Glu Lieu Ile Glu Lys Gly His Gly Ile Arg Lieu. Lieu. Glu Ala Glin Ile Ala Thr Gly Gly Ile Ile Asp Pro Lys Glu Ser His Arg Lieu Pro Val O Asp Ile Ala Tyr Lys Arg Gly Tyr Phe Asn. Glu Glu Lieu. Ser Glu OO Ile Lieu. Ser Asp Pro Ser Asp Asp Thir Lys Gly Phe Phe Asp Pro 24 O O Asn Thr Glu Glu Asn Lieu. Thir Tyr Lieu Gln Lieu Lys Glu Arg Cys 242O O Ile Lys Asp Glu Glu. Thr Gly Lieu. Cys Lieu. Lieu. Pro Leu Lys Glu O 2445 Llys Llys Lys Glin Val Glin Thir Ser Glin Lys Asn. Thir Lieu. Arg Llys O Arg Arg Val Val Ile Val Asp Pro Glu Thir Asn Lys Glu Met Ser Val Glin Glu Ala Tyr Lys Lys Gly Lieu. Ile Asp Tyr Glu Thir Phe 248O O Lys Glu Lieu. Cys Glu Glin Glu. Cys Glu Trp Glu Glu Ile Thir Ile OO 2505 Thr Gly Ser Asp Gly Ser Thr Arg Val Val Lieu Val Asp Arg Llys 251O O Thr Gly Ser Glin Tyr Asp Ile Glin Asp Ala Ile Asp O Llys Gly Lieu. Val Asp Arg Llys Phe Phe Asp Glin Tyr Arg Ser Gly Ser Lieu. Ser 254 O Lieu. Thr Glin Phe Ala Asp Met Ile Ser Lieu Lys Asn Gly Val Gly Thir Ser Ser Ser Met Gly Ser Gly Val Ser Asp Asp Val Phe Ser s 2580 Ser Ser Arg His Glu Ser Val Ser Lys Ile Ser Thr Ile Ser Ser Val Arg Asn Lieu. Thir Ile Arg Ser Ser Ser Phe Ser Asp Thir Lieu. 26 OO O Glu Glu Ser Ser Pro Ile Ala Ala Ile Phe Asp Thr Glu Asn Lieu O 262s Glu Lys Ile Ser Ile Thr Glu Gly Ile Glu Arg Gly Ile Val Asp 263 O O Ser Ile Thr Gly Glin Arg Lieu. Lieu. Glu Ala Glin Ala Cys Thr Gly

82 US 2008/ A1 Mar. 27, Continued Gly Ile Ile His Pro Thr Thr Gly Glin Llys Lieu Ser Leu Glin Asp 266 O Ala Val Ser Glin Gly Val Ile Asp Glin Asp Met Ala Thir Ser Val O 2685 Llys Pro Ala Glin Lys Ala Phe Ile Gly Phe Glu Gly Wall Lys Gly OO Llys Llys Llys Met Ser Ala Ala Glu Ala Val Lys Glu Lys Trp Lieu. 27 OS 271 O 2715 Pro Tyr Glu Ala Gly Glin Arg Phe Lieu. Glu Phe Glin 272O O Tyr Lieu. Thr Gly Gly Lieu Val Asp Pro Glu Val His Gly Arg Ile Ser Thr Glu O 2745 Glu Ala Ile Arg Lys Gly Phe Ile Asp Gly Arg Ala Ala Glin Arg s 276 O Lieu. Glin Asp Thir Ser Ser Tyr Ala Lys Ile Lieu. Thir Cys Pro Llys Thir Lys Lieu Lys Ile Ser Tyr Lys Asp Ala Ile Asn Arg Ser Met O Val Glu Asp Ile Thr Gly Lieu. Arg Lieu. Lieu. Glu Ala Ala Ser Val 2.79s 28OO 2805 Ser Ser Lys Gly Lieu Pro Ser Pro Tyr Asn Met Ser Ser Ala Pro O Gly Ser Arg Ser Gly Ser Arg Ser Gly Ser Arg Ser Gly Ser Arg O 2835 Ser Gly Ser Arg Ser Gly Ser Arg Arg Gly Ser Phe Asp Ala Thr 284 O O Gly Asn Ser Ser Tyr Ser Tyr Ser Tyr Ser Phe Ser Ser Ser Ser O 2865 Ile Gly His 2870 <210 SEQ ID NO 2 <211 LENGTH: 23 &212> TYPE: DNA <213> ORGANISM: Unknown &220s FEATURE: <223> OTHER INFORMATION: Oligonucleotide <4 OO SEQUENCE: 2 ggtcagttac gtgcagctga agg 23 <210 SEQ ID NO 3 <211 LENGTH: 18 &212> TYPE: DNA <213> ORGANISM: Unknown &220s FEATURE: <223> OTHER INFORMATION: Oligonucleotide <4 OO SEQUENCE: 3 gctgaggctg cc.ggat.cg 18 <210 SEQ ID NO 4 <211 LENGTH: 27 &212> TYPE: DNA <213> ORGANISM: Unknown &220s FEATURE:

83 US 2008/ A1 Mar. 27, Continued <223> OTHER INFORMATION: Oligonucleotide <4 OO SEQUENCE: 4 cgc.gc.ctcga gcc acatact ggtctgc 27 <210 SEQ ID NO 5 <211 LENGTH: 23 &212> TYPE: DNA <213> ORGANISM: Unknown &220s FEATURE: <223> OTHER INFORMATION: Oligonucleotide <4 OO SEQUENCE: 5 gcttagctgaggctg.ccgga t cq 23 <210 SEQ ID NO 6 <211 LENGTH: 16 &212> TYPE: PRT <213> ORGANISM: Unknown &220s FEATURE: <223> OTHER INFORMATION: N-terminal amino acids in expressed KBD-B <4 OO SEQUENCE: 6 Met Arg Gly Ser His His His His His His Gly Ser Ala Cys Glu Lieu O 15 <210 SEQ ID NO 7 <211 LENGTH: 10 &212> TYPE: PRT <213> ORGANISM: Unknown &220s FEATURE: <223> OTHER INFORMATION: C-terminal amino acids in expressed KBD-B <4 OO SEQUENCE: 7 Gly Val Asp Lieu. Glin Pro Ser Lieu. Ile Ser O <210 SEQ ID NO 8 <211 LENGTH: 56 &212> TYPE: DNA <213> ORGANISM: Unknown &220s FEATURE: <223> OTHER INFORMATION: Olionucleotide <4 OO SEQUENCE: 8 gctaaggaat t caccatgca toaccatcac cat cacgagc cacatactgg totgct 56 <210 SEQ ID NO 9 <211 LENGTH: 35 &212> TYPE: DNA <213> ORGANISM: Unknown &220s FEATURE: <223> OTHER INFORMATION: Oligonucleotide <4 OO SEQUENCE: 9 gctggaga at t ct cagctaa tta agcttgg Ctgca 35 <210 SEQ ID NO 10 <211 LENGTH: 50 &212> TYPE: DNA <213> ORGANISM: Unknown &220s FEATURE: <223> OTHER INFORMATION: Oligonucleotide

84 US 2008/ A1 Mar. 27, <4 OO SEQUENCE: 10 - Continued gctaaggaat tccatcacca toaccatcac gagccacata citggtctgct SO <210 SEQ ID NO 11 <211 LENGTH: 7 &212> TYPE: PRT <213> ORGANISM: Unknown &220s FEATURE: <223> OTHER INFORMATION: N-terminal amino acids in expressed KBD-B <4 OO SEQUENCE: 11 Met His His His His His His 1. 5 <210 SEQ ID NO 12 <211 LENGTH: 99 &212> TYPE: PRT <213> ORGANISM: Unknown &220s FEATURE: <223> OTHER INFORMATION: N-terminal amino acids in expressed KBD-B <4 OO SEQUENCE: 12 Met Arg Phe Pro Ser Ile Phe Thr Ala Val Lieu Phe Ala Ala Ser Ser O 15 Ala Lieu Ala Ala Pro Val Asn. Thir Thir Thr Glu Asp Glu Thir Ala Glin 2O 25 3O Ile Pro Ala Glu Ala Val Ile Gly Tyr Ser Asp Lieu. Glu Gly Asp Phe 35 4 O 45 Asp Wall Ala Val Lieu Pro Phe Ser Asn. Ser Thr Asn. Asn Gly Lieu. Lieu SO 55 6 O Phe Ile Asn. Thir Thir Ile Ala Ser Ile Ala Ala Lys Glu Glu Gly Val s 8O Ser Lieu. Glu Lys Arg Glu Ala Glu Ala Tyr Val Glu Phe His His His His His His <210 SEQ ID NO 13 <211 LENGTH: 10 &212> TYPE: PRT <213> ORGANISM: Unknown &220s FEATURE: <223> OTHER INFORMATION: N-terminal amino acids in expressed KBD-B <4 OO SEQUENCE: 13 Tyr Val Glu Phe His His His His His His O <210 SEQ ID NO 14 <211 LENGTH: 45 &212> TYPE: DNA <213> ORGANISM: Unknown &220s FEATURE: <223> OTHER INFORMATION: Oligonucleotide <4 OO SEQUENCE: 14 caccatgcat cac cat cacc at cacgagcc acatactggit ctdct 45 <210 SEQ ID NO 15 <211 LENGTH: 2O &212> TYPE: DNA

85 US 2008/ A1 Mar. 27, 2008 <213> ORGANISM: Unknown &220s FEATURE: <223> OTHER INFORMATION: Oligonucleotide <4 OO SEQUENCE: 15 gctaattaag Cttggctgca - Continued <210 SEQ ID NO 16 &2 11s LENGTH: 75 &212> TYPE: PRT <213> ORGANISM: Unknown &220s FEATURE: <223> OTHER INFORMATION: C-terminal amino acids <4 OO SEQUENCE: 16 Lys Gly Gly Arg Ala Asp Pro Ala Phe Lieu. Tyr Llys Val O Arg Lieu. Lieu. Thir Llys Pro Glu Arg Llys Lieu. Lieu. Glu Gly 2O 25 Thr Glin Lieu. Lieu. Phe Pro Lieu Val Arg Val Asn. Cys Ala 35 4 O 45 in expressed KBD-B Wall Gly 3O Luell Met Ile 15 Pro Gly Gly Val Ile Met Val Ile Ala Val Ser Cys Val Llys Lieu Lleu Ser SO 55 6 O Ser Thr Gln His Thr Ser Arg Llys His Llys Val s Ala His Asn 1. A cosmetic composition for treating keratin-containing materials, comprising at least one keratin-binding polypep tide sequence (i) in a cosmetically compatible medium. 2. The cosmetic composition according to claim 1, wherein the polypeptide sequence (i) has a binding affinity to human hair keratin, nail keratin, or skin keratin. 3. The cosmetic composition according to claim 1, wherein the polypeptide sequence (i) comprises at least one of the following polypeptide sequences, (a) the polypeptide sequence of SEQID NO:1 at position 2193 to 2481 (b) the polypeptide sequence of SEQID NO:1 at position 2606 to 2871 (c) a polypeptide sequence which is modified compared with (a) in up to 60% of the amino acids, (d) a polypeptide sequence which is modified compared with (b) in up to 50% of the amino acids, with the proviso that the keratin binding of polypeptide sequence (c) or (d) amounts to at least 10% of the value shown by polypeptide sequence (a) or (b), measured in the test as in example 9 or The cosmetic composition according to claim 1, which comprises the polypeptide sequence (i) in an amount of from 0.01 to 30% by weight. 5. The cosmetic composition according to claim 1, which, besides the polypeptide sequence (i), comprises at least one cosmetic active ingredient. 6. The cosmetic composition according to claim 5. wherein the cosmetic active ingredient is chosen from the group consisting of natural or synthetic polymers, pigments, moisturizers, oils, waxes, enzymes, minerals, vitamins, Sun screens, dyes, fragrances, antioxidants and preservatives. 7. A composition for improving the combability of hair comprising the cosmetic composition according to claim A composition for improving the setting of hair com prising the cosmetic composition according to claim A composition for a conditioning effect on the skin comprising the cosmetic composition according to claim A composition for preparing compositions for skin, nail and hair cosmetics comprising the cosmetic composi tion according to claim A pharmaceutical composition for treating keratin containing materials, comprising at least one keratin-binding polypeptide sequence (i) in a pharmaceutically compatible medium. 12. A keratin-binding effector molecule consisting of (i) at least one polypeptide sequence which has a binding affinity for a keratin, (ii) an effector molecule which is not naturally linked to the polypeptide sequence (i). 13. The keratin-binding effector molecule according to claim 12, where the polypeptide sequence (i) has binding affinity for the keratin of human hair, nails or skin. 14. The keratin-binding effector molecule according to claim 12, where the polypeptide sequence (i) includes at least one of the following polypeptide sequences, (a) the polypeptide sequence of SEQID NO:1 at position 2269 to 2508 (b) the polypeptide sequence of SEQID NO:1 at position 2606 to 2871 (c) a polypeptide sequence which is modified compared with (a) in up to 70% of the amino acids, (d) a polypeptide sequence which is modified compared with (b) in up to 70% of the amino acids,

86 US 2008/ A1 Mar. 27, 2008 with the proviso that the keratin binding of polypeptide sequence (c) or (d) amounts to at least 10% of the value shown by polypeptide sequence (a) or (b), measured in the assay described in example 9 or The keratin-binding effector molecule according to claim 12, where the effector molecule (ii) includes a polypeptide sequence. 16. The keratin-binding effector molecule according to claim 12, where the effector molecule (ii) has an enzymatic activity. 17. The keratin-binding effector molecule according to claim 12, where the effector molecule (ii) is a dye or a dye component. 18. The keratin-binding effector molecule according to claim 12, where the effector molecule (ii) is a UV filter. 19. The keratin-binding effector molecule according to claim 12, where the effector molecule (ii) is antioxidant. 20. The keratin-binding effector molecule according to claim 12, where the effector molecule (ii) is a carotenoid. 21. The keratin-binding effector molecule according to claim 12, where the effector molecule (ii) is a fungicide, insecticide or biocide. 22. The keratin-binding effector molecule according to claim 12, where the effector molecule (ii) is a vitamin or provitamin. 23. A composition for skin, nail and hair cosmetics comprising the keratin-binding effector molecules according to claim The keratin-binding effector molecule according to claim 12, where the effector molecule (ii) is attached to the polypeptide sequence (i) by covalent bonds. 25. The keratin-binding effector molecule according to claim 12, where the effector molecule (ii) is covalently bonded to functional groups of the side chain, the C-termi nus or the N-terminus of the polypeptide (i), utilizing two chemical functions already present in (i) and (ii). 26. The keratin-binding effector molecule according to claim 12, where one or more effector molecules (ii) is/are covalently bonded to functional groups of the side chain, the C-terminus or the N-terminus of the polypeptide (i), by way of an at least bifunctional linker. 27. The keratin-binding effector molecule according to claim 12, where a spacer element is incorporated between effector molecule (ii) and polypeptide (i). 28. The keratin-binding effector molecule according to claim 26 which has a potential cleavage site for a protease, lipase, esterase, phosphatase or hydrolase between effector molecule (ii) and polypeptide (i). 29. The keratin-binding effector molecule according to claim 26 which has a further polypeptide sequence which permits easy purification of the fusion protein between effector molecule (ii) and polypeptide (i). 30. A process for preparing the keratin-binding polypep tide sequence (i) according to claim A process for preparing the keratin-binding effector molecule according to claim 14. k k k k k