Coexisting order and disorder within a common 40-residue amyloid-β fibril structure in Alzheimer's disease brain tissue
文献情報
Ujjayini Ghosh, Wai-Ming Yau, Robert Tycko
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.
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Chemical Communications

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