Structural polymorphism of Alzheimer Aβ and other amyloid fibrils

Prion

Volumn 3, Issue 2, 2009, Pages 89-93

  Fändrich, Marcus ^a,d   Meinhardt, Jessica ^b   Grigorieff, Nikolaus ^c  

^a MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

^b FRITZ LIPMANN INSTITUTE   (Germany)

^c BRANDEIS UNIVERSITY   (United States)

^d MAX PLANCK RESEARCH UNIT FOR ENZYMOLOGY OF PROTEIN FOLDING   (Germany)

Author keywords

Aggregation; Alzheimer disease; Neurodegeneration; Prion; Protein folding

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN; POLYPEPTIDE;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; AMYLOIDOSIS; CREUTZFELDT JAKOB DISEASE; CRYSTAL STRUCTURE; HUMAN; HYDROGEN BOND; MORPHOLOGY; NON INSULIN DEPENDENT DIABETES MELLITUS; NOTE; PHYSICAL CHEMISTRY; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN POLYMORPHISM; PROTEIN STRUCTURE; TRANSMISSION ELECTRON MICROSCOPY; X RAY DIFFRACTION; ANIMAL; BIOLOGICAL MODEL; CHEMISTRY; METABOLISM; REVIEW;

ALZHEIMER DISEASE; AMYLOID; AMYLOID BETA-PROTEIN; ANIMALS; HUMANS; MODELS, BIOLOGICAL; PROTEIN CONFORMATION;

EID: 70349568356     PISSN: 19336896     EISSN: 1933690X     Source Type: Journal    
DOI: 10.4161/pri.3.2.8859     Document Type: Note

References (51)

1. Chiti F, Dobson CM. Protein misfolding, functional amyloid and human disease. Annu Rev Biochem 2006; 75:333-366 (Pubitemid 44118036)
2. Fändrich M. On the structural definition of amyloid fibrils and other polypeptide aggregates. Cell Mol Life Sci 2007; 64:2066-2078 (Pubitemid 350092423)
3. Sunde M, Serpell LC, Bartlam M, Fraser PE, Pepys MB, Blake CC. Common core structure of amyloid fibrils by synchrotron X-ray diffraction. J Mol Biol 1997; 273:729-739 (Pubitemid 27488813)
4. Fändrich M, Dobson CM. The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation. EMBO J 2002; 21:5682-5690 (Pubitemid 35315268)
5. Jimenez JL, Guijarro JI, Orlova E, Zurdo J, Dobson CM, Sunde M, et al. Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. EMBO J 1999; 18:815-821 (Pubitemid 29082261)
6. Jimenez JL, Nettleton EJ, Bouchard M, Robinson CV, Dobson CM, Saibil HR. The protofilament structure of insulin amyloid fibrils. Proc Natl Acad Sci USA 2002; 99:9196-9201 (Pubitemid 34764590)
7. Harper JD, Lieber CM, Lansbury PT Jr. Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein. Chem Biol 1997; 4:951-959 (Pubitemid 28050379)
8. Goldsbury CS, Wirtz S, Müller SA, Sunderji S, Wicki P, Aebi U, et al. Studies on the in vitro assembly of Aβ 1-40: implications for the search for Aβ fibril formation inhibitors. J Struct Biol 2000; 130:217-231
9. Chamberlain AK, MacPhee CE, Zurdo J, Morozova-Roche LA, Hill HA, Dobson CM, et al. Ultrastructural organization of amyloid fibrils by atomic force microscopy. Biophys J 2000; 79:3282-3293
10. Meinhardt J, Sachse C, Hortschansky P, Grigorieff N, Fändrich M. Aβ(1-40) fibril polymorphism implies diverse interaction patterns in amyloid fibrils. J Mol Biol 2009; 386:869-877
11. Bauer HH, Aebi U, Häner M, Hermann R, Müller M, Merkle HP. Architecture and polymorphism of fibrillar supramolecular assemblies produced by in vitro aggregation of human calcitonin. J Struct Biol 1995; 115:1-15.
12. Goldsbury CS, Cooper GJ, Goldie KN, Müller SA, Saafi EL, Gruijters WTM, et al. Polymorphic fibrillar assembly of human amylin. J Struct Biol 1997; 119:17-27. (Pubitemid 27294718)
13. Pedersen JS, Dikov D, Flink JL, Hjuler HA, Christiansen G, Otzen DE. The changing face of glucagon fibrillation: structural polymorphism and conformational imprinting. J Mol Biol 2006; 355:501-523 (Pubitemid 41785753)
14. Bouchard M, Zurdo J, Nettleton EJ, Dobson CM, Robinson CV. Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy. Protein Sci 2000; 9:1960-1967 (Pubitemid 30836563)
15. Dzwolak W, Smirnovas V, Jansen R, Winter R. Insulin forms amyloid in a straindependent manner: an FT-IR spectroscopic study. Protein Sci 2004; 13:1927-1932 (Pubitemid 38822132)
16. Petkova AT, Leapman RD, Guo Z, Yau WM, Mattson MP, Tycko R. Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils. Science 2005; 307:262-265 (Pubitemid 40116242)
17. Malinchik SB, Inouye H, Szumowski KE, Kirschner DA. Structural analysis of Alzheimer's β(1-40) amyloid: protofilament assembly of tubular fibrils. Biophys J 1998; 74:537-545
18. Jimenez JL, Tennent G, Pepys M, Saibil HR. Structural diversity of ex vivo amyloid fibrils studied by cryo-electron microscopy. J Mol Biol 2001; 311:241-247 (Pubitemid 32744538)
19. Crowther RA, Goedert M. Abnormal tau-containing filaments in neurodegenerative diseases. J Struct Biol 2000; 130:271-279 (Pubitemid 30679827)
20. Seilheimer B, Bohrmann B, Bondolfi L, Müller F, Stüber D, Döbeli H. The toxicity of the Alzheimer's β-amyloid peptide correlates with a distinct fiber morphology. J Struct Biol 1997; 119:59-71. (Pubitemid 27294721)
21. Meyer-Luehmann M, Coomaraswamy J, Bolmont T, Kaeser S, Schaefer C, Kilger E, et al. Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host. Science 2006; 313:1781-1784 (Pubitemid 44454153)
22. Diaz-Avalos R, King CY, Wall J, Simon M, Caspar DL. Strain-specific morphologies of yeast prion amyloid fibrils. Proc Natl Acad Sci USA 2005; 102:10165-10170 (Pubitemid 41023343)
23. Yamaguchi K, Takahashi S, Kawai T, Naiki H, Goto Y. Seeding-dependent propagation and maturation of amyloid fibril conformation. J Mol Biol 2005; 352:952-960 (Pubitemid 41267080)
24. Telling GC, Parchi P, DeArmond SJ, Cortelli P, Montagna P, Gabizon R, et al. Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity. Science 1996; 274:2079-2082 (Pubitemid 27020700)
25. Bessen RA, Kocisko DA, Raymond GJ, Nandan S, Lansbury PT, Caughey B. Nongenetic propagation of strain-specific properties of scrapie prion protein. Nature 1995; 375:698-700.
26. Toyama BH, Kelly MJ, Gross JD, Weissman JS. The structural basis of yeast prion strain variants. Nature 2007; 449:233-237 (Pubitemid 47402368)
27. Wickner RB, Edskes HK, Shewmaker F, Nakayashiki T. Prions of fungi: inherited structures and biological roles. Nat Rev Microbiol 2007; 5:611-618 (Pubitemid 47074116)
28. Cohen DL, Hedera P, Premkumar DR, Friedland RP, Kalaria RN. Amyloid-beta protein angiopathies masquerading as Alzheimer's disease? Ann N Y Acad Sci 1997; 826:390-395
29. Ikeda S, Yanagisawa N. Variable clinical manifestations of familial amyloid polyneuropathy and living related liver transplantation. Rinsho Shinkeigaku 1995; 35:1433-1435 (Pubitemid 26198845)
30. Goldsbury C, Frey P, Olivieri V, Aebi U, Müller SA. Multiple assembly pathways underlie amyloid-β fibril polymorphisms. J Mol Biol 2005; 352:282-298 (Pubitemid 41213315)
31. Ionescu-Zanetti C, Khurana R, Gillespie JR, Petrick JS, Trabachino LC, Minert LJ, et al. Monitoring the assembly of Ig light-chain amyloid fibrils by atomic force microscopy. Proc Natl Acad Sci USA 1999; 96:13175-13179
32. Heise H, Hoyer W, Becker S, Andronesi OC, Riedel D, Baldus M. Molecular-level secondary structure, polymorphism and dynamics of full-length a-synuclein fibrils studied by solid-state NMR. Proc Natl Acad Sci USA 2005; 102:15871-15876 (Pubitemid 41552835)
33. van der Wel PC, Lewandowski JR, Griffin RG. Solid-state NMR study of amyloid nanocrystals and fibrils formed by the peptide GNNQQNY from yeast prion protein Sup35p. J Am Chem Soc 2007; 129:5117-5130 (Pubitemid 46651390)
34. Madine J, Jack E, Stockley PG, Radford SE, Serpell LC, Middleton DA. Structural insights into the polymorphism of amyloid-like fibrils formed by region 20-29 of amylin revealed by solid-state NMR and X-ray fiber diffraction. J Am Chem Soc 2008; 130:14990-15001
35. Williams AD, Portelius E, Kheterpal I, Guo JT, Cook KD, Xu Y, et al. Mapping Aβ amyloid fibril secondary structure using scanning proline mutagenesis. J Mol Biol 2004; 335:833-842 (Pubitemid 38352823)
36. Petkova AT, Ishii Y, Balbach JJ, Antzutkin ON, Leapman RD, Delaglio F, et al. A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR. Proc Natl Acad Sci USA 2002; 99:16742-16747 (Pubitemid 36034043)
37. Williams AD, Shivaprasad S, Wetzel R. Alanine scanning mutagenesis of Aβ(1-40) amyloid fibril stability. J Mol Biol 2006; 357:1283-1294
38. Makarava N, Baskakov IV. The same primary structure of the prion protein yields two distinct self-propagating states. J Biol Chem 2008; 283:15988-15996
39. Verel R, Tomka IT, Bertozzi C, Cadalbert R, Kammerer RA, Steinmetz MO, et al. Polymorphism in an amyloid-like fibril-forming model peptide. Angew Chem Int Ed Engl 2008; 47:5842-5845
40. Klement K, Wieligmann K, Meinhardt J, Hortschansky P, Richter W, Fändrich M. Effect of different salt ions on the propensity of aggregation and on the structure of Alzheimer's Aβ(1-40) amyloid fibrils. J Mol Biol 2007; 373:1321-1333 (Pubitemid 47539491)
41. Peim A, Hortschansky P, Christopeit T, Schroeckh V, Richter W, Fändrich M. Mutagenic exploration of the cross-seeding and fibrillation propensity of Alzheimer's β-amyloid peptide variants. Protein Sci 2006; 15:1801-1805
42. Petkova AT, Ishii Y, Balbach JJ, Antzutkin ON, Leapman RD, Delaglio F, et al. A structural model for Alzheimer's beta-amyloid fibrils based on experimental constraints from solid state NMR. Proc Natl Acad Sci USA 2002; 99:16742-16747 (Pubitemid 36034043)
43. Lührs T, Ritter C, Adrian M, Riek-Loher D, Bohrmann B, Döbeli H, et al. 3D structure of Alzheimer's amyloid-β(1-42) fibrils. Proc Natl Acad Sci USA 2005; 102:17342-17347
44. Whittemore NA, Mishra R, Kheterpal I, Williams AD, Wetzel R, Serpersu EH. Hydrogendeuterium (H/D) exchange mapping of Aβ 1-40 amyloid fibril secondary structure using nuclear magnetic resonance spectroscopy. Biochemistry 2005; 44:4434-4441 (Pubitemid 40403985)
45. Sawaya MR, Sambashivan S, Nelson R, Ivanova MI, Sievers SA, Apostol MI, et al. Atomic structures of amyloid cross-β spines reveal varied steric zippers. Nature 2007; 447:453-457 (Pubitemid 46816731)
46. Anfinsen CB. Principles that govern the folding of protein chains. Science 1973; 181:223-230
47. Dobson CM, Sali A, Karplus M. Protein folding: a perspective from theory and experiment. Angew Chem Int Ed 1998; 37:868-893 (Pubitemid 28228882)
48. Chiti F, Webster P, Taddei N, Clark A, Stefani M, Ramponi G, et al. Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc Natl Acad Sci USA 1999; 96:3590-3594 (Pubitemid 29168954)
49. Fändrich M, Fletcher MA, Dobson CM. Amyloid fibrils from muscle myoglobin. Nature 2001; 410:165-166
50. Krebs MR, Macphee CE, Miller AF, Dunlop IE, Dobson CM, Donald AM. The formation of spherulites by amyloid fibrils of bovine insulin. Proc Natl Acad Sci USA 2004; 101:14420-14424 (Pubitemid 39346764)
51. Wetzel R, Shivaprasad S, Williams AD. Plasticity of amyloid fibrils. Biochemistry 2007; 46:1-10. (Pubitemid 46075018)