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      The molecular structure of Alzheimer β-amyloid fibrils formed in the presence of phospholipid vesicles.

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          Abstract

          β-amyloid (Aβ) fibrils are the major species involved in Alzheimer's disease (AD). An atomic-resolution molecular structure of Aβ40 fibrils formed in the presence of lipid vesicles was obtained by using magic angle spinning (MAS) solid-state NMR spectroscopy. The fibril structures formed in the presence of the lipid vesicles are remarkably different from those formed in solution. These results provide insights into the molecular mechanism of Aβ aggregation in the presence of lipid vesicles.

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          Author and article information

          Journal
          Angew. Chem. Int. Ed. Engl.
          Angewandte Chemie (International ed. in English)
          1521-3773
          1433-7851
          Aug 25 2014
          : 53
          : 35
          Affiliations
          [1 ] Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, Wuhan Center for Magnetic Resonance, Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, Wuhan, 430071 (P.R. China).
          Article
          10.1002/anie.201311106
          24810551
          9a41a4fa-d878-43c2-ab29-6b66672fdbfb
          © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
          History

          Alzheimer’s disease,NMR spectroscopy,magic-angle spinning,protein structures,β-amyloid aggregation

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