formation Jan Bieschke Max Delbrück Centrum für Molekulare Medizin, Berlin NeuroProteomics
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1 Molecular l intervention ti into amyloid formation Jan Bieschke Max Delbrück Centrum für Molekulare Medizin, Berlin NeuroProteomics
2 Protein misfolding diseases - Common features of protein folding diseases - Molecular mechanisms (Alzheimer, Parkinson, polyq disorders, systemic amyloidosis) - Therapeutic strategies for amyloid diseases (anti-aggregation therapies)
3 Formation of insoluble protein aggregates g is a common feature of amyloid diseases Clinical syndrome Oligomer/aggregate component Alzheimer s disease Amyloid-ß (Aß) peptide PD HD Huntington s disease Huntingtin, or huntingtin fragments Parkinson s disease - Synuclein Spongiform Prion, or prion fragments encephalopathies Type II diabetes Fragment of IAPP AD
4 Amyloid Fibrillogenesis Amyloid- Huntingtin Prion protein Synuclein
5 Mechanism of amyloid formation nucleation growth unstructured misfolded nucleus, n* monomer monomer amyloid
6 Mechanism of amyloid formation nucleation growth unstructured misfolded nucleus, n* monomer monomer Seeded Unseeded Amyloid markers: amyloid Aggregatio on Dye binding (Thioflavin T, Congo Red) Resistance to denaturation Time
7 Toxic A amyloid intermediates nucleation growth spherical agg. protofibrils fibrils Toxicity rel. metabolic rat te 1 18h 0h oligo fibril Fu, Bieschke & Kelly JACS 2005 Bieschke, et al. Biochemistry 2008
8 Aging-related insulin and stress response pathways modulate amyloid toxicity it Cohen & Bieschke, Science 2006 Stress response (HSF-1) Insulin/IGF receptor FOXO transcription factor Disaggregation Active aggregation monomer small diffusible aggregate large aggregate
9 Anti-amyloid intervention strategies 1 nucleation growth Prevent amyloid formation / stabilize monomer 2. Destabilize amyloid: -sheet breaker, congo red 3. Induce amyloid aggregate fomation (on-pathway) 4. Redirect amyloid aggregate formation (off-pathway)
10 Anti-amyloid intervention strategies 1 nucleation growth 1. Prevent amyloid formation / stabilize monomer: -Secretase inhibitors TTR-stabilizing drugs
11 dissociation misfolding amyloid growth Science 2003
12 Anti-amyloid intervention strategies 1 nucleation growth Prevent amyloid formation / stabilize monomer 2. Destabilize amyloid: -sheet breaker, congo red 3. Induce amyloid aggregate fomation (on-pathway) 4. Redirect amyloid aggregate formation (off-pathway)
13 Redirecting amyloid aggregate formation (off- pathway) nucleation growth Inducing the formation of non-amyloid aggregates reduces toxic oligomer and fibrillar species: Epigallochatechin-3-gallate (EGCG)
14 EGCG and GCG inhibit huntingtin aggregation Ehrnhöfer et al. Hum. Mol. Gen. 2006
15 EGCG induces the formation of spherical / amorphous aggregates SS A 42 control EGCG 100 Ehrnhöfer & Bieschke et al. Nature Struct. Mol. Biol. 2008
16 Anti-oligomer antibody A11 does not recognize EGCG-generated aggregates unstructured monomer misfolded monomer nucleus, n* amyloid yod Anti oligomer (Kayed et al. Science 2003) Anti A
![[arb b] F ( 6000](/docs-images/76/73216813/images/17-3.jpg "4000 2000 0 0 10")
17 EGCG-induced aggregates do not bind Thioflavin EGCG : A ratio x 0.1x 0.5x 1x 5x 10x ThT) [arb b] F ( t[ [h]
18 EGCG induced and aggregates are not seeding-competent Amyloid seed + + Unstructured oligomer Monomers Fibril Time (h)
![toxic to PC12 cells %]](/docs-images/76/73216813/images/19-2.jpg "tivity [% bolic act")
19 EGCG-induced A 42 aggregates are not toxic to PC12 cells %] tivity [% bolic act Cell metab
20 Model of EGCG induced off-pathway aggregation
21 Future directions: Can small molecules disassemble amyloid fibrils? Fibrillar oligomer Drug modified fibril
22 Future directions: Clinical efficacy of EGCG in amyloid diseases Possible therapeutic benefit of EGCG in light chain amyloidosis (Hunstein, Blood 2007) Planned clinical trials in LC-amyloidosis, systemic Transthyretin amyloidosis, Huntington s disease, Alzheimers disease German clinical green tea consortium
23 Acknowledgements Max Delbrück Centrum Berlin Susanne Kostka Gerlinde Grelle Katja Welsch Jenny Russ Maliha Shah Heike Wobst Ralf Friedrich The Scripps Research Institute Sarah Siegel Yanwen Fu Prof. Jeffery Kelly The Salk Institute Ehud Cohen Prof. Andrew Dillin Dagmar Ehrnhöfer Martin Herbst Prof. Erich Wanker Funding NGFN Helmholtz Gemeinschaft NeuroProteomics
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