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Updated: Aug 15, 2026

Enrichment of Detergent-insoluble Protein Aggregates from Human Postmortem Brain
Published on: October 24, 2017
Coexisting order and disorder within a common 40-residue amyloid-β fibril structure in Alzheimer's disease brain
Ujjayini Ghosh1, Wai-Ming Yau, Robert Tycko
1Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Building 5, Room 409, Bethesda, Maryland 20892-0520, USA. robertty@mail.nih.gov.
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.
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