CHEMO SENSORS. C.P. Rao
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1 CHEM SESS C.P. ao Bio-Inorganic Chemistry Group Department of Chemistry Indian Institute of Technology Bombay August 04, 2010
2 Acknowledgements oymon Balaji Amitabha Jugun akesh Sreenivasu Khatija Anil Jayaraman Vijay Atanu Amit Department of Chemistry & IIT Bombay Central facilities of IIT Bombay SAIF Funding: DST, CSI, DAE-BS
3 Carbohydrate based switch-on molecular sensor for Cu(II) in buffer: Absorption and fluorescence study of the selective recognition of Cu(II) ions by galactosyl derivative in HEPES buffer. C.P. ao and Co-workers, rg. Lett., 8 (2006)
4 Biological Inorganic Chemistry ole of Metal ions in Biological systems Proteins ucleic acids Carbohydrates Metal ions which activate proteins: a +, K +, Ca 2+, Mg 2+ Metalloproteins (binds through covalent bonds): Mn 2+/5+, Fe 2+/3+, Co 2+, i 2+, Cu 2+, Zn 2+,Mo +3/+6, V +3/+5, W +3/+6 (found in organisms live in high temperature volcanos)
5 Types of Zinc enzymes 1. xidoreductases 2. Hydrolases 3. Transferases 4. Peptidases 5. Lyases 6. Ligases Zinc containing proteins Carboxypeptidase A PDB #: 1M4L
6 Copper containing proteins (Type-2 Cu) (Type-3 Cu) 2 Type 1 Type 2 (Type-1 Cu) Laccase Type 3
7 Iron containing Proteins Heme proteins 2 transport : H b & M b e - transfer : cytochromes xygenation Monoxygenases :Cytochrome P450 Dioxygenases : trp-2,3-deoxygenase on-heme proteins 2 transport : hemerythrins e - transport : Fe-S proteins xygenases Mono : Di : Catechol-dioxygenase Deoxygenases: ibonucleotide reductase Storage : Ferritin Cytochrome P450
8 Bimetallic enzymes M (n+1)+ SD + 2 M n+ SD + 2 Cu/Zn - Superoxide dismutase
9 Specificity & Selectivity towards metal ions ecognition Binding eactivity
10 Platforms to develop Chemo Sensors based on calix[4]arene based on carbohydrates Appropriate binding cores are to be built
11 Binding core development H H H H H H H H H H H H H H
12 on-selective recognition of diamine derivative H 2 H 2 Fluorescence sensitive towards heavy metal ions, H H viz., Hg 2+, Cd 2+ & Pb 2+ Cannot be differentiated either on emission or absorption properties Well built binding cores are needed H H H H H H H H H H H H Hg 2+, Cd 2+ & Pb 2+ C.P ao & coworkers, J. Photochem. Photobiol. A, 2007, 188, 325
13 ecognition of Fe 2+ ~ Cu 2+ >>> Zn 2+ by imine-anthracenyl derivative Intensity Zn 2+ Fe 2+ Cu 2+ Zn 2+ Co 2+ i 2+ Mg 2+ Mn 2+ L Wavelength, nm Sensitivity: Fe 2+ ~ Cu 2+ >>> Zn 2+ Imine moiety is responsible for binding Lower rim phenolic core at best can help once the binding takes place through imine moiety I/I [M 2+ ]/[L 7 ] I/I M 2+ /L 8 Fe 2+ Cu 2+ Zn 2+ H H L 9 Fe 2+ Cu 2+ C.P ao & coworkers, J. Photochem. Photobiol. Photochem. A, 177, 2006, 164
14 Zn 2+ sensing by Calix-Schiff s base conjugate Tetrahedron Lett., 46 (2005) 7967 Intensity Wavelength, nm I/I H H HC CH H H L [Zn 2+ ]/[L 6 ] I/I Ti 4+ V 2+ Cr 3+ Mn 2+ Fe 2+ Co 2+ i 2+ Cu 2+ Zn 2+ Cd 2+ Hg 2+ Mg 2+ Ti Vo Cr Mn Fe Co i Cu Zn Cd HgMg
15 Binding core modifications: Variations in the sensing of Zn 2+ Mg I 0 /I I/I Mn 2+ Fe 2+ Co 2+ i 2+ Cu 2+ Zn 2+ a + K + Ca 2+ L 2 L 3 L 4 Mg 2+ H H H H L 2 H H H H H H L 3 H H H H L 4 Absorbance Wavelength, nm Absorbance L L 3 L Wavelength, nm Absorbance Wavelength, nm
![Structural evidence for the Zinc complex of L 4 1 2 H H Zn H H Zn(Ac) 2 CH 2 Cl 2, CH 3 H 2 1 L 4 [ZnL 4 ] 2 A-B (Å) A-B-C (º) Zn Zn 9.39 1-Zn-2 106.](/docs-images/93/111749364/images/16-0.jpg "98 Zn 1 1.91 1-Zn-1 125.53 Zn 2 1.90 1-Zn-2 96.49 Zn 2 1.96 2-Zn-1 94.59 Zn 1 1.98 2-Zn-2 125.53 C.P. ao & coworkers Unpublished results 1-Zn-2 110.")
16 Structural evidence for the Zinc complex of L H H Zn H H Zn(Ac) 2 CH 2 Cl 2, CH 3 H 2 1 L 4 [ZnL 4 ] 2 A-B (Å) A-B-C (º) Zn Zn Zn Zn Zn Zn Zn Zn Zn Zn Zn C.P. ao & coworkers Unpublished results 1-Zn
17 Colorimetric sensing of Fe 2+ and Cu 2+ by L 4 L4 is non-selective using fluorescence emission Can be selectively sensed by absorption spectrosocpy L L+Mn 2+ L+Fe 2+ L+Co 2+ L+i 2+ L+Cu 2+ L+Zn 2+ L+Ca 2+ L+Mg 2+ L+a + L+K + L = L Absorbance Fe 2+ Cu Wavelength, nm Wavelength, nm H L 4 H H H
18 atification of sensing by DFT Computations
19 Binding core comparisons H H H H H H H H H H H H H H H H H H on Selective Exhibits fluorescence changes with Cd 2+, Hg 2+ and Pb 2+ on Selective Fluorescence trend follows the order Fe 2+ ~ Cu 2+ >>> Zn 2+ Selective for Zn fold fl. enhancement Forming 1:1 L 2.Zn 2+ complex K a = 1.2 x 10 5 M -1 Detection limit = 60 ppb Zinc complex acts as amino Selective for Zn Fold fl. enhancement Forming 1:1 L 3 Zn 2+ complex K a = 2.02 x 10 6 M -1 Detection limit = 192 ppb Zinc complex used for Selective for Zn 2+ & Cu 2+ 8 Fold fl. Enhancement with Zn 2+ Forming 2:2 L 4 Zn 2+ complex K a = 6.98 x 10 4 M fold quenching with Cu 2+ K a = 2.08 x 10 4 M -1 acid sensor phosphate & amino acid Detection limit = 480 ppb detection Colorimetric detection of Cu 2+ & Fe 2+
20 Fluorescence switch-on sensor for Zn 2+ in blood serum milieu Fluorescence Intensity I/I [Zn 2+ ]/[L] L L+Zn Wavelength (nm) C.P. ao and co-workers, Chem. Comm. 46 (2010)
21 ole of additional binding moieties in the core on Zn 2+ sensing C.P. ao and co-workers, Tetrahedron Letts., 50 (2009)
![2+ ] Fl.](/docs-images/93/111749364/images/22-4.jpg "quenching fold 25 20 15 10 5")
22 Zn 2+ complex as dual sensor for Amino acid and Phosphate H H H H H H I/I H 2-2 P 4- HP 3-4 P [Anion]/[L+Zn 2+ ] Fl. quenching fold Ala Arg Asn Asp Cys Glu Gln Gly His IIe Leu Lys Met Phe Pro Ser Thr Try Tyr Val IHIBIT logic gate Zn 2+ I 450 HP 4 2- C.P ao & coworkers, J. rg. Chem. 2010, 75, 3387
![jacalin}, (c) PA, (d) {[ZnL] +](/docs-images/93/111749364/images/23-4.jpg "PA}. C.P. ao and co-workers, J.")
23 Transfer of Zn 2+ from these sensors to proteins: Causing aggregational changes This transfer is facilitated through the interactions of the side chains of Asp, Glu & Cys to Zn 2+ (a) (b) (c) (d) AFM pictures of (a) jacalin, (b) {[ZnL] + jacalin}, (c) PA, (d) {[ZnL] + PA}. C.P. ao and co-workers, J. Phys. Chem. B., 113 (2009)
24 Extending this to dual sensing of i 2+ & Zn 2+ C.P. ao and Co-workers, Tetrahedron. Letts., 49 (2008)
25 Homometallic and hetero bi-metallic complexes B3LYP/6-31G* Distorted h Distorted T d B3LYP/6-31G* Distorted T d HF/3-21G C.P. ao and Co-workers, Tetrahedron. Letts., 49 (2008) Distorted Tbp
26 Sensor for Ag + L L+Ag + L+Ag + +Cys XD Ag-L C.P. ao and Co-workers, J. rg. Chem. 74 (2009)
27 Sensor for Hg 2+ in aqueous acetonitrile L L + Hg 2+ L L + Hg 2+ C.P. ao and Co-workers, J. rg. Chem. 73 (2008)
28 Sensor for Cu 2+ XD Control molecules B3LYP/6-31G* Plastocyanin C.P. ao and co-workers, Tetrahedron Letts., 50 (2009)
29 Sensor for amino acids, peptides and proteins Amino acids I0 /I I/I 0 Val C4A-Et C4A-H C4A-Phe-Me C4A-Phe-H C4A-Gly-H C4A-Ala-H Lys Leu Asn Gln Met Arg Ser Pro His Ilu Thr Ala Cys Gly Phe Glu Asp C-Phe-H I 0 /I I/I 0 {L+ Glu} {L + [GSH-AgP]} {L+ lactalbumin} {L -Me+ lactalbumin} anosphere formed by two hexameric units of {L + Glu}
30 Carbohydrates based sensors
31 aked eye chemo sensor for Fe 3+ B3LYP/6-31G* L 1 In Methanol Lig Ca 2+ Mg 2+ Mn 2+ Fe 2+ Fe 3+ Co 2+ i 2+ Cu 2+ Zn 2+ Cd 2+ Hg 2+ L 2 L 1 In Aq. HEPES Buffer L 2 Lig Ca 2+ Mg 2+ Mn 2+ Fe 2+ Fe 3+ Co 2+ i 2+ Cu 2+ Zn 2+ Cd 2+ Hg 2+ C.P. ao and co-workers, Tetrahedron. Letts., 50 (2009)
32 Sensor for Cu 2+ di-(cu-l 3 ) di-(cu-l 1 ) C.P. ao and Co-workers, Dalton Transactions (2009)
33 Sensors for Amino acids H H H H H H C.P. ao and co-workers J. rg. Chem., 72 (2007)
34 Amino acid recognition Specific & on-specific H H H H H B3LYP/6-311+G(d,p) HCH 2 (GI) H H 2 Alanine CH 2 Specific H 2 Lysine H H on-specific CH 2 H H SH Cysteine H H C.P. ao and co-workers J. rg. Chem., 72 (2007)
35 ecognition of galactose by jacalin: Gal-a1-6Glc bound structure BBA, 2002, 1572, 198
36 Chemo sensor for aromatic amino acids L+Trp L+His B3LYP/6-31G L+Phe L+Tyr C.P. ao and co-workers, Tetrahedron Lett. 51 (2010)
37 ano fibers formed through π π Interactions L+Phe (T-=0) L+Phe (T=8 h) L+Phe (T=8 h) L+Phe (T=8 h) TEM H TEM L+Phe (T-=0) L+Phe (T=8 h) L+Phe (T=24 h) C.P. ao and co-workers, ACS ano 4 (2010)
38 Differentiating α-helical & β-sheet Proteins by nano fibers [L+Phe]+BSA [L+Phe]+HSA [L+Phe]+Lactalbumin
39 H H H H H HH 2 H H (i) Inhibition of glycosidases H H H H H H (i) (ii) H H H H 2 H H H H 1 1a 1b/1c H H H H 2 3 3a 3c H H (iii) H H H H H H H 2.HCl (ii) 4a H µcal/sec kcal/mol of injectant H H (i) H H H HH 2a (ii) Time (min) H (ii) H 2 H 4b / 4c H H /' H H H H ' '= HH 2b/2c = Time (min) C.P. ao and co-workers, Glycoconjugates J. 26(4) (2009) /' H H /' H H Time (min) Mixture of enzymes (1c) (1b) (2c) (2b) Molar atio Molar atio Molar atio Molar atio (μmol) Time (min) Pure mannosidase
40 αg + 1c Glyco-conjugate binding analysis HαM+ 1c o. of interactions Asp GluCys Trp TyrPhe Arg SerLys Amino acid Met Asn IleAla Leu % E S a1b1c 2 2a2b2c 3 3c4a4b4c Glyco-conjugates o. of Interactions Ar C.P ao and co-workers Glyco-conjugates J. 26(4) (2009)
41 Conclusions & correlations Cu 2+ /Ag + i 2+ /Zn 2+ Zn 2+ Zn 2+ Hg 2+ H H H H H H Asp/Glu/GSH BSA, HSA Lactalbumin -P 4 2- Asp, Glu, His, Cys BSA, HSA, Jacalin, PA Asp, Cys HP 4 2-
42 GI Cu 2+, Glu (mainly), His GA Ala, Lys, Cys Glu-2-SI Glu-2-I Zn 2+, His, Trp, Phe Zn 2+, Cu 2+, Fe 3+
43
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