Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation.
Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation.
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淀粉样β纤维的原子分辨率三维结构带有大阪突变。
DOI：
10.1002/anie.201408598
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发表时间：
2015-01-02
期刊：
影响因子：
--
通讯作者：
Meier BH
中科院分区：
文献类型：
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作者：
Schütz AK;Vagt T;Huber M;Ovchinnikova OY;Cadalbert R;Wall J;Güntert P;Böckmann A;Glockshuber R;Meier BH
尽管其对于理解阿尔茨海默病（AD）的分子基础至关重要，但与AD密切相关的淀粉样β肽（Aβ）原纤维的高分辨率结构信息却很少。我们报告了与早发性AD相关的Aβ1-40肽Osaka突变（E22Δ）的原子分辨率原纤维结构。的结构，这与所有以前提出的模型有很大的不同，是基于大量的明确的内和分子间的固态NMR距离的限制。
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.