Amyloid formation via supramolecular peptide assemblies

Biochemistry

Volumn 46, Issue 24, 2007, Pages 7079-7087

  Moore, Roger A ^a   Hayes, Stanley F ^a   Fischer, Elizabeth R ^a   Priola, Suzette A ^a  

^a NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; DYES; MOLECULAR STRUCTURE; OPTICAL PROPERTIES; PEPTIDES; SUPRAMOLECULAR CHEMISTRY;

AMYLOID FIBRILS; CONGO RED; FIBRILLIZATION;

STARCH;

AMYLOID; AMYLOID BETA PROTEIN[1-40]; CONGO RED; PRION PROTEIN;

ARTICLE; BETA SHEET; NONHUMAN; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; SUPRAMOLECULAR CHEMISTRY; ULTRASTRUCTURE;

AMYLOID; AMYLOID BETA-PROTEIN; ANIMALS; CRICETINAE; HUMANS; MICROSCOPY, ELECTRON; MICROSCOPY, ELECTRON, SCANNING; MODELS, MOLECULAR; MULTIPROTEIN COMPLEXES; PEPTIDE FRAGMENTS; PRIONS; RECOMBINANT PROTEINS; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 34250858885     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700247y     Document Type: Article

References (40)

1. Merlini, G., and Bellotti, V. (2003) Molecular mechanisms of amyloidosis, N. Engl. J. Med. 349, 583-596.
2. Zerovnik, E. (2002) Amyloid-fibril formation. Proposed mechanisms and relevance to conformational disease, Eur. J. Biochem. 269, 3362-3371.
3. Surewicz, W. K., Jones, E. M., and Apetri, A. C. (2006) The emerging principles of mammalian prion propagation and transmissibility barriers: Insight from studies in vitro, Acc. Chem. Res. 39, 654-662.
4. Nilsson, M. R. (2004) Techniques to study amyloid fibril formation in vitro, Methods 34, 151-160.
5. Baskakov, I. V., Legname, G., Baldwin, M. A., Prusiner, S. B., and Cohen, F. E. (2002) Pathway complexity of prion protein assembly into amyloid, J. Biol. Chem. 277, 21140-21148.
6. Yamin, G., Uversky, V. N., and Fink, A. L. (2003) Nitration inhibits fibrillation of human α-synuclein in vitro by formation of soluble oligomers, FEBS Lett. 542, 147-152.
7. Collins, S. R., Douglass, A., Vale, R. D., and Weissman, J. S. (2004) Mechanism of prion propagation: Amyloid growth occurs by monomer addition, PLoS Biol. 2, e321.
8. Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., and Glabe, C. G. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis, Science 300, 486-489.
9. Kirkitadze, M. D., Bitan, G., and Teplow, D. B. (2002) Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies, J. Neurosci. Res. 69, 567-577.
10. Bitan, G., Fradinger, E. A., Spring, S. M., and Teplow, D. B. (2005) Neurotoxic protein oligomers: What you see is not always what you get, Amyloid 12, 88-95.
11. Cleary, J. P., Walsh, D. M., Hofmeister, J. J., Shankar, G. M., Kuskowski, M. A., Selkoe, D. J., and Ashe, K. H. (2005) Natural oligomers of the amyloid-β protein specifically disrupt cognitive function, Nat. Neurosci. 8, 79-84.
12. Souillac, P. O., Uversky, V. N., and Fink, A. L. (2003) Structural transformations of oligomeric intermediates in the fibrillation of the immunoglobulin light chain LEN, Biochemistry 42, 8094-8104.
13. Walsh, D. M., Hartley, D. M., Kusumoto, Y., Fezoui, Y., Condron, M. M., Lomakin, A., Benedek, G. B., Selkoe, D. J., and Teplow, D. B. (1999) Amyloid β-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates, J. Biol. Chem. 274, 25945-25952.
14. Kayed, R., Sokolov, Y., Edmonds, B., McIntire, T. M., Milton, S. C., Hall, J. E., and Glabe, C. G. (2004) Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases, J. Biol. Chem. 279, 46363-46366.
15. Lashuel, H. A., Hartley, D., Petre, B. M., Walz, T., and Lansbury, P. T., Jr. (2002) Neurodegenerative disease: Amyloid pores from pathogenic mutations, Nature 418, 291.
16. Demuro, A., Mina, E., Kayed, R., Milton, S. C., Parker, I., and Glabe, C. G. (2005) Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers, J. Biol. Chem. 280, 17294-17300.
17. Zhu, M., Han, S., Zhou, F., Carter, S. A., and Fink, A. L. (2004) Annular oligomeric amyloid intermediates observed by in situ atomic force microscopy, J. Biol. Chem. 279, 24452-24459.
18. Catharino, S., Buchner, J., and Walter, S. (2005) Characterization of oligomeric species in the fibrillization pathway of the yeast prion Ure2p, Biol. Chem. 386, 633-641.
19. Dong, J., Apkarian, R. P., and Lynn, D. G. (2005) Imaging amyloid β peptide oligomeric particles in solution, Bioorg. Med. Chem. 13, 5213-5217.
20. Mastrangelo, I. A., Ahmed, M., Sato, T., Liu, W., Wang, C., Hough, P., and Smith, S. O. (2006) High-resolution atomic force microscopy of soluble Aβ342 oligomers, J. Mol. Biol. 358, 106-119.
21. Petkova, A. T., Leapman, R. D., Guo, Z., Yau, W. M., Mattson, M. P., and Tycko, R. (2005) Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils, Science 307, 262-265.
22. Colucci, M., Moleres, F. J., Xie, Z. L., Ray-Chaudhury, A., Gutti, S., Butefisch, C. M., Cervenakova, L., Wang, W., Goldfarb, L. G., Kong, Q., Ghetti, B., Chen, S. G., and Gambetti, P. (2006) Gerstmann-Straussler-Scheinker: A new phenotype with 'curly' PrP deposits, J. Neuropathol. Exp. Neurol. 65, 642-651.
23. Ghetti, B., Piccardo, P., Spillantini, M. G., Ichimiya, Y., Porro, M., Perini, F., Kitamoto, T., Tateishi, J., Seiler, C., Frangione, B., Bugiani, O., Giaccone, G., Prelli, F., Goedert, M., Dlouhy, S. R., and Tagliavini, F. (1996) Vascular variant of prion protein cerebral amyloidosis with τ-positive neurofibrillary tangles: The phenotype of the stop codon 145 mutation in PRNP, Proc. Natl. Acad. Sci. U.S.A. 93, 744-748.
24. Moore, R. A., Herzog, C., Errett, J., Kocisko, D. A., Arnold, K. M., Hayes, S. F., and Priola, S. A. (2006) Octapeptide repeat insertions increase the rate of protease-resistant prion protein formation, Protein Sci. 15, 609-619.
25. Zahn, R., von Schroetter, C., and Wuthrich, K. (1997) Human prion proteins expressed in Escherichia coli and purified by high-affinity column refolding, FEBS Lett. 417, 400-404.
26. Rochet, J. C., and Lansbury, P. T., Jr. (2000) Amyloid fibrillo-genesis: Themes and variations, Curr. Opin. Struct. Biol. 10, 60-68.
27. Sipe, J. D., and Cohen, A. S. (2000) Review: History of the amyloid fibril, J. Struct. Biol. 130, 88-98.
28. Serpell, L. C., Sunde, M., and Blake, C. C. (1997) The molecular basis of amyloidosis, Cell. Mol. Life Sci. 53, 871-887.
29. Sipe, J. D. (1992) Amyloidosis, Annu. Rev. Biochem. 61, 947-975.
30. Seshadri, S., Khurana, R., and Fink, A. L. (1999) Fourier transform infrared spectroscopy in analysis of protein deposits, Methods Enzymol. 309, 559-576.
31. Kyte, J., and Doolittle, R. F. (1982) A simple method for displaying the hydropathic character of a protein, J. Mol. Biol. 157, 105-132.
32. Soreghan, B., Kosmoski, J., and Glabe, C. (1994) Surfactant properties of Alzheimer's Aβ peptides and the mechanism of amyloid aggregation, J. Biol. Chem. 269, 28551-28554.
33. Sluzky, V., Tamada, J. A., Klibanov, A. M., and Langer, R. (1991) Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces, Proc. Natl. Acad. Sci. U.S.A. 88, 9377-9381.
34. Serio, T. R., Cashikar, A. G., Kowal, A. S., Sawicki, G. J., Moslehi, J. J., Serpell, L., Arnsdorf, M. F., and Lindquist, S. L. (2000) Nucleated conformational conversion and the replication of conformational information by a prion determinant, Science 289, 1317-1321.
35. Khurana, R., Coleman, C., Ionescu-Zanetti, C., Carter, S. A., Krishna, V., Grover, R. K., Roy, R., and Singh, S. (2005) Mechanism of thioflavin T binding to amyloid fibrils, J. Struct. Biol. 151, 229-238.
36. Pauling, L., and Corey, R. B. (1951) The pleated sheet, a new layer configuration of polypeptide chains, Proc. Natl. Acad. Sci. U.S.A. 37, 251-256.
37. Daggett, V. (2006) α-Sheet: The Toxic Conformer in Amyloid Diseases? Acc. Chem. Res. 39, 594-602.
38. Westlind-Danielsson, A., and Arnerup, G. (2001) Spontaneous in vitro formation of supramolecular β-amyloid structures, "βamy balls", by β-amyloid 1-40 peptide, Biochemistry 40, 14736-14743.
39. Hamodrakas, S. J., Hoenger, A., and Iconomidou, V. A. (2004) Amyloid fibrillogenesis of silkmofh chorion protein peptide-analogues via a liquid-crystalline intermediate phase, J. Struct. Biol. 145, 226-235.
40. Barghorn, S., Nimmrich, V., Striebinger, A., Krantz, C., Keller, P., Janson, B., Bahr, M., Schmidt, M., Bitner, R. S., Harlan, J., Barlow, E., Ebert, U., and Hillen, H. (2005) Globular amyloid β-peptide oligomer: A homogenous and stable neuropathological protein in Alzheimer's disease, J. Neurochem. 95, 834-847.