Stabilization of Solvent to α-Sheet Structure and Conversion Between α-Sheet and β-Sheet in the Fibrillation Process of Amyloid Peptide.
Stabilization of Solvent to α-Sheet Structure and Conversion Between α-Sheet and β-Sheet in the Fibrillation Process of Amyloid Peptide.
复制标题
淀粉样肽原纤维化过程中溶剂对 α-片层结构的稳定以及 α-片层和 β-片层之间的转换。
DOI：
10.1021/acs.jpcb.9b07903
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发表时间：
2019
期刊：
影响因子：
--
通讯作者：
Fei Li
中科院分区：
文献类型：
--
作者：
Feihong Meng;Tong Lu;Fei Li
α-折叠构象被认为是淀粉样蛋白的中间构象组分，在一定条件下介导淀粉样蛋白的纤维状组装。然而，在淀粉样变性机制的研究中，由于α-折叠中间体的存在以及α-折叠中间体向β-折叠纤维转变的证据不足，对这种构象的关注较少。本文对一种D，L-交替淀粉样蛋白十肽在不同条件下的结构进行了表征，并研究了该肽在原纤化过程中α-折叠和β-折叠之间的结构转换。首次获得了水溶液中α-折叠结构原纤的图像，并发现水分子在α-折叠结构稳定中的重要作用。我们还提供了肽聚集体中α-折叠向β-折叠结构转变的实验证据。
Alpha-sheet conformation has been proposed to exist as an intermediate conformational component and mediate the fibrillar assemblies of amyloid proteins at certain conditions. However, less attention has been paid to this form of conformation in the studies of the mechanism of amyloidosis because there is insufficient evidence for the existence of α-sheet intermediate and the transition from α-sheet intermediate to β-sheet fibril. Herein, we characterized the structures of a D,L-alternating amyloidogenic decapeptide under different conditions and studied the structural conversion between α-sheet and β-sheet in the fibrillation processes of the peptide. We obtained for the first time the image of α-sheet structured fibrils in aqueous solution and found the essential role of water molecules in the stabilization of the α-sheet structure. We also provided experimental evidence of the structural conversion from α-sheet to β-sheet in the peptide aggregates.
影响因子：
2.9
作者：
VENUGOPAL, MG;RAMSHAW, JAM;BRODSKY, B
通讯作者：
BRODSKY, B
影响因子：
5.6
作者：
Kellock J;Hopping G;Caughey B;Daggett V
通讯作者：
Daggett V