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

ABSTRACT

Fibrils formed by 40- and 42-residue amyloid-ß (Aß40 and Aß42) peptides exhibit molecular-level structural polymorphisms. A recent screen of fibrils derived from brain tissue of Alzheimer's disease patients revealed a single predominant Aß40 polymorph. We present solid state nuclear magnetic resonance (ssNMR) data that define its coexisting structurally ordered and disordered segments.