Kinetic Intermediates in Amyloid Assembly
Kinetic Intermediates in Amyloid Assembly
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DOI：
10.1021/ja508621b
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发表时间：
2014-10-29
影响因子：
15
通讯作者：
Lynn, David G.
中科院分区：
文献类型：
--
作者：
Liang, Chen;Ni, Rong;Lynn, David G.
与预期的淀粉样蛋白组装的奥斯特瓦尔德样成熟相反，阿尔茨海默病的A β肽的荷兰突变体的成核核心通过一系列构象转变组装。通过同位素编辑的IR和固态NMR对中间体组装体进行结构表征，揭示了意想不到的链取向中间体，并提出了渐进组装途径中的新成核机制。
In contrast to an expected Ostwald-like ripening of amyloid assemblies, the nucleating core of the Dutch mutant of the A beta peptide of Alzheimers disease assembles through a series of conformational transitions. Structural characterization of the intermediate assemblies by isotope-edited IR and solid-state NMR reveals unexpected strand orientation intermediates and suggests new nucleation mechanisms in a progressive assembly pathway.