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Title: Atomic-resolution 3D structure of amyloid β fibrils: The Osaka mutation

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
Authors:
 [1] ;  [2] ;  [3] ;  [1] ;  [3] ;  [1] ;  [4] ;  [5] ;  [3] ;  [1]
  1. ETH Zurich, Wolfgang-Pauli-Strasse. Zurich (Switzerland)
  2. Brookhaven National Lab. (BNL), Upton, NY (United States)
  3. ETH Zurich, Zurich (Switzerland)
  4. Goethe Univ., Frankfurt (Germany)
  5. Univ. de Lyon, Lyon (France)
Publication Date:
OSTI Identifier:
1183283
Report Number(s):
BNL--107758-2015-JA
Journal ID: ISSN 1433-7851; R&D Project: BO-108; KP1501010
Grant/Contract Number:
SC00112704
Type:
Accepted Manuscript
Journal Name:
Angewandte Chemie (International Edition)
Additional Journal Information:
Journal Name: Angewandte Chemie (International Edition); Journal Volume: 54; Journal Issue: 1; Journal ID: ISSN 1433-7851
Publisher:
Wiley
Research Org:
Brookhaven National Laboratory (BNL), Upton, NY (United States)
Sponsoring Org:
USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES