Assembly of Alzheimer's Aβ peptide into nanostructured amyloid fibrils

Current Opinion in Colloid and Interface Science

Volumn 16, Issue 6, 2011, Pages 508-514

  Morgado, Isabel ^a   Fändrich, Marcus ^a  

^a MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

Author keywords

Aggregation; Inhibitor; Prion; Protein folding

Indexed keywords

ALZHEIMER; ALZHEIMER'S DISEASE; AMYLOID DISEASE; AMYLOID FIBRIL; BIOPHYSICAL TECHNIQUES; INHIBITOR; NANO-STRUCTURED; NEURODEGENERATIVE; PRION; SINGLE-PARTICLE; STRUCTURE DETERMINATION; TRANSIENT STABILIZATION;

AGGLOMERATION; GLYCOPROTEINS; PEPTIDES; PROTEIN FOLDING;

NEURODEGENERATIVE DISEASES;

AMYLOID BETA PROTEIN; BINDING PROTEIN; DIPEPTIDE; EPIGALLOCATECHIN GALLATE; NANOMATERIAL;

BIOPHYSICS; COGNITIVE DEFECT; DRUG EFFECT; HUMAN; NONHUMAN; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN STRUCTURE; REACTION ANALYSIS; REVIEW; STRUCTURE ANALYSIS;

EID: 84855795920     PISSN: 13590294     EISSN: 18790399     Source Type: Journal    
DOI: 10.1016/j.cocis.2011.06.016     Document Type: Review

References (50)

1. Fändrich M., Schmidt M., Grigorieff N. Recent progress in understanding Alzheimer's β-amyloid structures. Trends Biochem Sci 2011, 36:338-345.
2. Finder V.H., Glockshuber R. Amyloid-beta aggregation. Neurodegener Dis 2007, 4:13-27.
3. Greenwald J., Riek R. Biology of amyloid: structure, function, andregulation. Structure 2010, 18:1244-1260.
4. Broersen K., Rousseau F., Schymkowitz J. The culprit behind amyloid beta peptide related neurotoxicity in Alzheimer's disease: oligomer size or conformation?. Alzheimers Res Ther 2010, 2:12.
5. Butterfield S.M., Lashuel H.A. Amyloidogenic protein-membrane interactions: mechanistic insight from model systems. Angew Chem Int Ed Engl 2010, 49:5628-5654.
6. Terzi E., Holzemann G., Seelig J. Self-association of β-amyloid peptide (1-40) in solution and binding to lipid membranes. J Mol Biol 1995, 252:633-642.
7. Terzi E., Holzemann G., Seelig J. Interaction of Alzheimer β-amyloid peptide (1-40) with lipid membranes. Biochemistry 1997, 36:14845-14852.
8. Hou L., Shao H., Zhang Y., Li H., Menon N.K., Neuhaus E.B., et al. Solution NMR studies of the Aβ(1-40) and Aβ(1-42) peptides establish that the Met35 oxidation state affects the mechanism of amyloid formation. J Am Chem Soc 2004, 126. 1992-05.
9. Vitalis A., Caflisch A. Micelle-Like architecture of the monomer ensemble of Alzheimer's amyloid-β peptide in aqueous solution and its implications for Aβ aggregation. J Mol Biol 2010, 403:148-165.
10. 42 in liquid water. J Chem Phys 2008, 129:195101-195111.
11. Tew D.J., Bottomley S.P., Smith D.P., Ciccotosto G.D., Babon J., Hinds M.G., et al. Stabilization of neurotoxic soluble β-sheet-rich conformations of the Alzheimer's disease amyloid-β peptide. Biophys J 2008, 94:2752-2766.
12. Dahse K., Garvey M., Kovermann M., Vogel A., Balbach J., Fändrich M., et al. DHPC strongly affects the structure and oligomerization propensity of Alzheimer's Aβ(1-40) peptide. J Mol Biol 2010, 403:643-659.
13. Wahlstrom A., Hugonin L., Peralvarez-Marin A., Jarvet J., Graslund A. Secondary structure conversions of Alzheimer's Aβ(1-40) peptide induced by membrane-mimicking detergents. FEBS J 2008, 275:5117-5128.
14. Sticht H., Bayer P., Willbold D., Dames S., Hilbich C., Beyreuther K., et al. Structure of amyloid A4-(1-40)-peptide of Alzheimer's disease. Eur J Biochem 1995, 233:293-298.
15. Maltseva E., Kerth A., Blume A., Möhwald H., Brezesinski G. Adsorption of amyloid β (1-40) peptide at phospholipid monolayers. Chembiochem 2005, 6:1817-1824.
16. Sachse C., Grigorieff N., Fändrich M. Nanoscale flexibility parameters of Alzheimer amyloid fibrils determined by electron cryo-microscopy. Angew Chem Int Ed Engl 2010, 49:1321-1323.
17. Paravastu A.K., Leapman R.D., Yau W.M., Tycko R. Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils. Proc Natl Acad Sci USA 2008, 105:18349-18354.
18. 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.
19. Kodali R., Williams A.D., Chemuru S., Wetzel R. Aβ(1-40) forms five distinct amyloid structures whose β-sheet contents and fibril stabilities are correlated. J Mol Biol 2010, 401:503-517.
20. Schmidt M., Sachse C., Richter W., Xu C., Fändrich M., Grigorieff N. Comparison of Alzheimer Aβ(1-40) and Aβ(1-42) amyloid fibrils reveals similar protofilament structures. Proc Natl Acad Sci USA 2009, 106:19813-19818.
21. Sachse C., Fändrich M., Grigorieff N. Paired β-sheet structure of an Aβ(1-40) amyloid fibril revealed by electron microscopy. Proc Natl Acad Sci USA 2008, 105:7462-7466.
22. Saraiva A.M., Pereira M.C., Brezesinski G. Is the viscoelasticity of Alzheimer's Aβ42 peptide oligomers a general property of protein oligomers related to their toxicity?. Langmuir 2010, 26:12060-12067.
23. Sandberg A., Luheshi L.M., Söllvander S., Pereira de Barros T., Macao B., Knowles T.P.J., et al. Stabilization of neurotoxic Alzheimer amyloid-β oligomers by protein engineering. Proc Natl Acad Sci USA 2010, 107:15595-15600.
24. Habicht G., Haupt C., Friedrich R.P., Hortschansky P., Sachse C., Meinhardt J., et al. Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Aβ protofibrils. Proc Natl Acad Sci USA 2007, 104:19232-19237.
25. Eckert A., Hauptmann S., Scherping I., Meinhardt J., Rhein V., Dröse S., et al. Oligomeric and fibrillar species of β-amyloid (Aβ42) both impair mitochondrial function in P301L tau transgenic mice. J Mol Med 2008, 86:1255-1267.
26. 1-42 oligomers to fibrils. Nat Struct Mol Biol 2010, 17:561-567.
27. Chimon S., Shaibat M.A., Jones C.R., Calero D.C., Aizezi B., Ishii Y. Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's β-amyloid. Nat Struct Mol Biol 2007, 14:1157-1164.
28. Glabe C.G. Structural classification of toxic amyloid oligomers. J Biol Chem 2008, 283:29639-29643.
29. Goldsbury C.S., Wirtz S., Müller S.A., Sunderji S., Wicki P., Aebi U., et al. Studies on the in vitro assembly of Aβ(1-40): implications for the search for Abeta fibril formation inhibitors. J Struct Biol 2000, 130:217-231.
30. Harper J.D., Wong S.S., Lieber C.M., Lansbury P.T. Observation of metastable Aβ amyloid protofibrils by atomic force microscopy. Chem Biol 1997, 4:119-125.
31. Walsh D.M., Hartley D.M., Kusumoto Y., Fezoui Y., Condron M.M., Lomakin A., et al. Amyloid β-protein fibrillogenesis. J Biol Chem 1999, 274:25945-25952.
32. Scheidt H.A., Morgado I., Rothemund S., Huster D., Fändrich M. Solid-state NMR spectroscopic investigation of Aβ protofibrils: implication of a β-sheet remodeling upon maturation into terminal amyloid fibrils. Angew Chem Int Ed Engl 2011, 50:2837-2840.
33. Harper J.D., Lansbury P.T. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu Rev Biochem 1997, 66:385-407.
34. Fändrich M. Absolute correlation between lag time and growth rate in the spontaneous formation of several amyloid-like aggregates and fibrils. J Mol Biol 2007, 365:1266-1270.
35. Knowles T.P.J., Waudby C.A., Devlin G.L., Cohen S.I.A., Aguzzi A., Vendruscolo M., et al. An analytical solution to the kinetics of breakable filament assembly. Science 2009, 326:1533-1537.
36. Xue W.F., Homans S.W., Radford S.E. Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly. Proc Natl Acad Sci USA 2008, 105:8926-8931.
37. Auer S., Meersman F., Dobson C.M., Vendruscolo M. A generic mechanism of emergence of amyloid protofilaments from disordered oligomeric aggregates. PLoS Comput Biol 2008, 4:e1000222.
38. Pellarin R., Schuetz P., Guarnera E., Caflisch A. Amyloid fibril polymorphism is under kinetic control. J Am Chem Soc 2010, 132:14960-14970.
39. Pellarin R., Caflisch A. Interpreting the aggregation kinetics of amyloid peptides. J Mol Biol 2006, 360:882-892.
40. Gsponer J., Haberthur U., Caflisch A. The role of side-chain interactions in the early steps of aggregation: molecular dynamics simulations of an amyloid-forming peptide from the yeast prion Sup35. Proc Natl Acad Sci USA 2003, 100:5154-5159.
41. 2-microglobulin. J Biol Chem 2009, 284:2169-2175.
42. Kellermayer M.S., Karsai A., Benke M., Soos K., Penke B. Stepwise dynamics of epitaxially growing single amyloid fibrils. Proc Natl Acad Sci USA 2008, 105:141-144.
43. Ban T., Hoshino M., Takahashi S., Hamada D., Hasegawa K., Naiki H., et al. Direct observation of Aβ amyloid fibril growth and inhibition. J Mol Biol 2004, 344:757-767.
44. Andersen C.B., Yagi H., Manno M., Martorana V., Ban T., Christiansen G., et al. Branching in amyloid fibril growth. Biophys J 2009, 96:1529-1536.
45. Ehrnhoefer D.E., Bieschke J., Boeddrich A., Herbst M., Masino L., Lurz R., et al. EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers. Nat Struct Mol Biol 2008, 15:558-566.
46. Haupt C., Bereza M., Kumar S.T., Kieninger B., Morgado I., Hortschansky P., et al. Pattern recognition with a fibril-specific antibody fragment reveals the surface variability of natural amyloid fibrils. J Mol Biol 2011, 408:529-540.
47. Luheshi L.M., Hoyer W., de Barros T.P., van Dijk Hard I., Brorsson A.C., Macao B., et al. Sequestration of the Aβ peptide prevents toxicity and promotes degradation in vivo. PLoS Biol 2010, 8(e1000334).
48. Andreetto E., Yan L.-M., Tatarek-Nossol M., Velkova A., Frank R., Kapurniotu A. Identification of hot regions of the Aβ-IAPP interaction interface as high-affinity binding sites in both cross- and self-association. Angew Chem Int Ed Engl 2010, 49:3081-3085.
49. Frydman-Marom A., Rechter M., Shefler I., Bram Y., Shalev D.E., Gazit E. Cognitive-performance recovery of Alzheimer's disease model mice by modulation of early soluble amyloidal assemblies. Angew Chem Int Ed Engl 2009, 48:1981-1986.
50. Friedrich R.P., Tepper K., Rönicke R., Soom M., Westermann M., Reymann K., et al. Mechanism of amyloid plaque formation suggests an intracellular basis of Aβ pathogenicity. Proc Natl Acad Sci USA 2010, 107:1942-1947.