Coexisting order and disorder within a common 40-residue amyloid-β fibril structure in Alzheimer's disease brain tissue
Coexisting order and disorder within a common 40-residue amyloid-β fibril structure in Alzheimer's disease brain tissue
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DOI：
10.1039/c8cc01967c
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发表时间：
2018-05-18
影响因子：
4.9
通讯作者：
Tycko, Robert
中科院分区：
文献类型：
--
作者：
Ghosh, Ujjayini;Yau, Wai-Ming;Tycko, Robert
由40-和42-残基淀粉样β（A β 40和A β 42）肽形成的原纤维表现出分子水平的结构多态性。最近对来自阿尔茨海默病患者脑组织的原纤维的筛选揭示了单一的主要A β 40多晶型。我们提出了固态核磁共振（ssNMR）数据，定义其共存的结构有序和无序的部分。
Fibrils formed by 40- and 42-residue amyloid-beta (A beta 40 and A beta 42) peptides exhibit molecular-level structural polymorphisms. A recent screen of fibrils derived from brain tissue of Alzheimer's disease patients revealed a single predominant A beta 40 polymorph. We present solid state nuclear magnetic resonance (ssNMR) data that define its coexisting structurally ordered and disordered segments.