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Article

Structural variation in amyloid-β fibrils from Alzheimer's disease clinical subtypes.

Nature - 12 Jan 2017

Qiang Wei, Yau Wai-Ming, Lu Jun-Xia, Collinge John, Tycko Robert

Abstract excerpt

Aggregation of amyloid-β peptides into fibrils or other self-assembled states is central to the pathogenesis of Alzheimer's disease. Fibrils formed in vitro by 40- and 42-residue amyloid-β peptides (Aβ40 and Aβ42) are polymorphic, with variations in molecular structure that depend on fibril growth conditions. Recent experiments suggest that variations in amyloid-β fibril structure in vivo may correlate with...

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Identifiers

PMID: 28052060
DOI: 10.1038/nature20814
PMCID: PMC5233555

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