| Literature DB >> 29707712 |
Ujjayini Ghosh1, 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.Entities:
Mesh:
Substances:
Year: 2018 PMID: 29707712 PMCID: PMC5953852 DOI: 10.1039/c8cc01967c
Source DB: PubMed Journal: Chem Commun (Camb) ISSN: 1359-7345 Impact factor: 6.222