Amyloid β-sheet mimics that antagonize protein aggregation and reduce amyloid toxicity

Nature Chemistry

Volumn 4, Issue 11, 2012, Pages 927-933

  Cheng, Pin Nan ^a   Liu, Cong ^b   Zhao, Minglei ^b   Eisenberg, David ^b   Nowick, James S ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; MACROCYCLIC COMPOUND; PEPTIDOMIMETIC AGENT;

ANIMAL; ARTICLE; CELL SURVIVAL; CHEMICAL STRUCTURE; CHEMISTRY; DRUG DESIGN; DRUG EFFECT; HUMAN; PC12 CELL; PROTEIN MULTIMERIZATION; PROTEIN SECONDARY STRUCTURE; RAT; SYNTHESIS;

AMYLOID BETA-PEPTIDES; ANIMALS; CELL SURVIVAL; DRUG DESIGN; HUMANS; MACROCYCLIC COMPOUNDS; MODELS, MOLECULAR; PC12 CELLS; PEPTIDOMIMETICS; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; RATS;

EID: 84867878408     PISSN: 17554330     EISSN: 17554349     Source Type: Journal    
DOI: 10.1038/nchem.1433     Document Type: Article

References (36)

1. Chiti, F. & Dobson, C. M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75, 333-366 (2006).
2. Aguzzi, A. & O'Connor, T. Protein aggregation diseases: pathogenicity and therapeutic perspectives. Nature Rev. Drug. Discov. 9, 237-248 (2010).
3. Bartolini, M. & Andrisano, V. Strategies for the inhibition of protein aggregation in human diseases. ChemBioChem 11, 1018-1035 (2010).
4. Greenwald, J. & Riek, R. Biology of amyloid: structure, function, and regulation. Structure 18, 1244-1260 (2010).
5. Tycko, R. Solid-state NMR studies of amyloid fibril structure. Annu. Rev. Phys. Chem.62, 279-299 (2011).
6. Eichner, T. & Radford, S. E. A diversity of assembly mechanisms of a generic amyloid fold. Mol. Cell 43, 8-18 (2011).
7. Lopez de la Paz, M. & Serrano, L. Sequence determinants of amyloid fibril formation. Proc. Natl Acad. Sci. USA 101, 87-92 (2004).
8. Goldschmidt, L., Teng, P. K., Riek, R. & Eisenberg, D. Identifying the amylome, proteins capable of forming amyloid-like fibrils. Proc. Natl Acad. Sci. USA 107, 3487-3492 (2010).
9. Nelson, R. et al. Structure of the cross-b spine of amyloid-like fibrils. Nature 435, 773-778 (2005).
10. Sawaya, M. R. et al. Atomic structures of amyloid cross-b spines reveal varied steric zippers. Nature 447, 453-457 (2007).
11. Conway, K. A. et al. Acceleration of oligomerization, not fibrillization, is a shared property of both a-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy. Proc. Natl Acad. Sci. USA 97, 571-576 (2000).
12. Lashuel, H. A., Hartley, D., Petre, B. M., Walz, T. & Lansbury, P. T. Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature 418, 291-291 (2002).
13. Chimon, S. et al. Evidence of fibril-like b-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's b-amyloid. Nature Struct. Mol. Biol. 14, 1157-1164 (2007).
14. Bernstein, S. L. et al. Amyloid-b protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease. Nature Chem. 1, 326-331 (2009).
15. Ono, K., Condron, M. M. & Teplow D. B. Structure-neurotoxicity relationships of amyloid b-protein oligomers. Proc. Natl Acad. Sci. USA 106, 14745-14750 (2009).
16. Woods, R. J. et al. Cyclic modular b-sheets. J. Am. Chem. Soc. 129, 2548-2558 (2007).
17. Liu, C. et al. Characteristics of amyloid-related oligomers revealed by crystal structures of macrocyclic b-sheet mimics. J. Am. Chem. Soc. 133, 6736-6744 (2011).
18. Zheng, J. et al. Macrocyclic b-sheet peptides that inhibit the aggregation of a tau-protein-derived hexapeptide. J. Am. Chem. Soc. 133, 3144-3157 (2011).
19. Gellman, S. H. Minimal model systems for b-sheet secondary structure in proteins. Curr. Opin. Chem. Biol. 2, 717-725 (1998).
20. Nowick, J. S. et al. An unnatural amino acid that mimics a tripeptide b-strand and forms b-sheetlike hydrogen-bonded dimers. J. Am. Chem. Soc. 122, 7654-7661 (2000).
21. Nowick, J. S. & Brower, J. O. A new turn structure for the formation of b-hairpins in peptides. J. Am. Chem. Soc. 125, 876-877 (2003).
22. Finder, V. H. & Glockshuber, R. Amyloid-b aggregation. Neurodegen. Dis. 4, 13-27 (2007).
23. Walsh, P., Simonetti, K. & Sharpe, S. Core structure of amyloid fibrils formed by residues 106-126 of the human prion protein. Structure 17, 417-426 (2009).
24. Friedhoff, P., von Bergen, M., Mandelkow, E-M., Davies, P. & Mandelkow, E. A nucleated assembly mechanism of Alzheimer paired helical filaments. Proc. Natl Acad. Sci. USA 95, 15712-15717 (1998).
25. 2-microglobulin important for nucleation and elongation of aggregation. J. Mol. Biol. 378, 251-263 (2008).
26. Vilar, M. et al. The fold of a-synuclein fibrils. Proc. Natl Acad. Sci. USA 105, 8637-8642 (2008).
27. Luca, S., Yau, W-M., Leapman, R. & Tycko, R. Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR. Biochemistry 46, 13505-13522 (2007).
28. Cheng, P-N. & Nowick, J. S. Giant macrolactams based on b-sheet peptides. J. Org. Chem. 76, 3166-3173 (2011).
29. Yan, L-M., Velkova, A., Tatarek-Nossol, M., Andreetto, E. & Kapurniotu, A. IAPP mimic blocks Ab cytotoxic self-assembly: cross-suppression of amyloid toxicity of Ab and IAPP suggests a molecular link between Alzheimer's disease and type II diabetes. Angew. Chem. Int. Ed. 46, 1246-1252 (2007).
30. Seeliger, J. et al. Cross-amyloid interaction of Ab and IAPP at lipid membranes. Angew. Chem. Int. Ed. 51, 679-683 (2012).
31. Ma, B. & Nussinov, R. Selective molecular recognition in amyloid growth and transmission and cross-species barriers. J. Mol. Biol. 421, 172-184 (2012).
32. Miller, Y., Ma, B. & Nussinov, R. Polymorphism in Alzheimer Ab amyloid organization reflects conformational selection in a rugged energy landscape. Chem. Rev. 110, 4820-4838 (2010).
33. Stains, C. I., Mondal, K. & Ghosh, I. Molecules that target beta-amyloid. ChemMedChem 2, 1674-1692 (2007).
34. Sciarretta, K. L., Gordon, D. J. & Meredith, S. C. Peptide-based inhibitors of amyloid assembly. Methods Enzymol. 413, 273-312 (2006).
35. Colletier, J-P. et al. Molecular basis for amyloid-b polymorphism. Proc. Natl Acad. Sci. USA 108, 16938-16943 (2011).
36. Laganowsky, A. et al. Atomic view of a toxic amyloid small oligomer. Science 335, 1228-1231 (2012).