Coexisting order and disorder within a common 40-residue amyloid-? fibril structure in Alzheimer's disease brain tissue.
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ABSTRACT:
SUBMITTER: Ghosh U
PROVIDER: S-EPMC5953852 | biostudies-literature | 2018 May
REPOSITORIES: biostudies-literature
Publications
Coexisting order and disorder within a common 40-residue amyloid-β fibril structure in Alzheimer's disease brain tissue.
Ghosh Ujjayini U Yau Wai-Ming WM Tycko Robert R
Chemical communications (Cambridge, England) 20180501 40
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. ...[more]
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