Atomic-resolution 3D structure of amyloid β fibrils: The Osaka mutation
Journal Article
·
· Angewandte Chemie (International Edition)
- ETH Zurich, Wolfgang-Pauli-Strasse. Zurich (Switzerland)
- Brookhaven National Lab. (BNL), Upton, NY (United States)
- ETH Zurich, Zurich (Switzerland)
- Goethe Univ., Frankfurt (Germany)
- Univ. de Lyon, Lyon (France)
Despite its central importance for understanding the molecular basis of Alzheimer's disease (AD), high-resolution structural information on amyloid β-peptide (Aβ) fibrils, which are intimately linked with AD, is scarce. We report an atomic-resolution fibril structure of the Aβ 1-40 peptide with the Osaka mutation (E22Δ), associated with early-onset AD. The structure, which differs substantially from all previously proposed models, is based on a large number of unambiguous intra- and intermolecular solid-state NMR distance restraints
- Research Organization:
- Brookhaven National Laboratory (BNL), Upton, NY (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23)
- OSTI ID:
- 1183283
- Report Number(s):
- BNL--107758-2015-JA; KP1501010
- Journal Information:
- Angewandte Chemie (International Edition), Journal Name: Angewandte Chemie (International Edition) Journal Issue: 1 Vol. 54; ISSN 1433-7851
- Publisher:
- WileyCopyright Statement
- Country of Publication:
- United States
- Language:
- English
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