Atomic‐Resolution Three‐Dimensional Structure of Amyloid β Fibrils Bearing the Osaka Mutation |
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| Authors: | Dr. Anne K. Schütz Dr. Toni Vagt Dr. Matthias Huber Dr. Oxana Y. Ovchinnikova Riccardo Cadalbert Dr. Joseph Wall Prof. Dr. Peter Güntert Dr. Anja Böckmann Prof. Dr. Rudi Glockshuber Prof. Dr. Beat H. Meier |
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| Affiliation: | 1. Physical Chemistry, ETH Zürich, Vladimir‐Prelog‐Weg 2, 8093 Zurich (Switzerland);2. Institute of Molecular Biology and Biophysics, ETH Zurich, Otto‐Stern‐Weg 5, 8093 Zurich (Switzerland);3. Brookhaven National Laboratory, 50 Bell Avenue, Building 463,Upton, NY 11973‐5000 (USA);4. Institute of Biophysical Chemistry, Center for Biomolecular Magnetic Resonance and Frankfurt Institute for Advanced Studies, Goethe University, Frankfurt am Main (Germany);5. Institut de Biologie et Chimie des Protéines, Bases Moléculaires et Structurales des Systèmes Infectieux, Labex Ecofect, UMR 5086 CNRS, Université de Lyon, 7 passage du Vercors, 69367 Lyon (France) |
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| Abstract: | 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 Aβ1‐40 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. |
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| Keywords: | Alzheimer's disease amyloids solid‐state NMR spectroscopy structure elucidation |
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