Coexisting order and disorder within a common 40-residue amyloid-β fibril structure in Alzheimer's disease brain tissue

Literature Information

Publication Date 2018-04-24
DOI 10.1039/C8CC01967C
Impact Factor 6.222
Authors

Ujjayini Ghosh, Wai-Ming Yau, Robert Tycko



Abstract

Fibrils formed by 40- and 42-residue amyloid-β (Aβ40 and Aβ42) peptides exhibit molecular-level structural polymorphisms. A recent screen of fibrils derived from brain tissue of Alzheimer's disease patients revealed a single predominant Aβ40 polymorph. We present solid state nuclear magnetic resonance (ssNMR) data that define its coexisting structurally ordered and disordered segments.

Source Journal

Chemical Communications

Chemical Communications
CiteScore: 8.6
Self-citation Rate: 4.7%
Articles per Year: 2458

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