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The Molecular Structure of Alzheimer β‐Amyloid Fibrils Formed in the Presence of Phospholipid Vesicles
Author(s) -
Niu Zheng,
Zhao Weijing,
Zhang Zhengfeng,
Xiao Fanshu,
Tang Xinqi,
Yang Jun
Publication year - 2014
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201311106
Subject(s) - vesicle , fibril , chemistry , magic angle spinning , phospholipid , biophysics , amyloid fibril , lipid bilayer , amyloid (mycology) , nuclear magnetic resonance spectroscopy , crystallography , amyloid β , biochemistry , stereochemistry , membrane , biology , medicine , disease , pathology , inorganic chemistry
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.