title: Recent progress in understanding Alzheimer's β-amyloid structures.
abstract: The formation of amyloid fibrils, protofibrils and oligomers from the β-amyloid (Aβ) peptide represents a hallmark of Alzheimer's disease. Aβ-peptide-derived assemblies might be crucial for disease onset, but determining their atomic structures has proven to be a major challenge. Progress over the past 5 years has yielded substantial new data obtained with improved methodologies including electron cryo-microscopy and NMR. It is now possible to resolve the global fibril topology and the cross-β sheet organization within protofilaments, and to identify residues that are crucial for stabilizing secondary structural elements and peptide conformations within specific assemblies. These data have significantly enhanced our understanding of the mechanism of Aβ aggregation and have illuminated the possible relevance of specific conformers for neurodegenerative pathologies.
authors.affiliation: Max-Planck Research Unit for Enzymology of Protein Folding & Martin-Luther University Halle-Wittenberg, Halle (Saale), Germany. fandrich@enzyme-halle.mpg.de
authors.forename: Marcus
authors.initials: M
authors.lastname: Fändrich
authors.forename: Matthias
authors.initials: M
authors.lastname: Schmidt
authors.forename: Nikolaus
authors.initials: N
authors.lastname: Grigorieff
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism* / Q000473:pathology; D000682:Amyloid / Q000737:chemistry / Q000378:metabolism; D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D006801:Humans; D011487:Protein Conformation
chemical_list: D000682:Amyloid; D016229:Amyloid beta-Peptides