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Recent progress in understanding Alzheimer's β-amyloid structures

TitleRecent progress in understanding Alzheimer's β-amyloid structures
Publication TypeJournal Article
Year of Publication2011
AuthorsFändrich, M, Schmidt M, Grigorieff N
Refereed DesignationRefereed
JournalTrends Biochem. Sci.
Volume36
Pagination338-45
Date Published2011 Mar 14
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 5years 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.

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