阿尔茨海默病β淀粉样肽折叠与二聚化的内在及环境影响
Internal and environmental effects on folding and dimerization of the Alzheimer's β amyloid peptide.
作者信息
Anand Priya, Hansmann Ulrich H E
机构信息
Department of Physics, Michigan Technological University, Houghton, MI 49931, USA.
出版信息
Mol Simul. 2011 May 1;37(6). doi: 10.1080/08927022.2011.551879.
Abstract
Amyloid deposits are a hallmark of many diseases. In the case of Alzheimer's disease a turn between 21Ala and 30Ala, stabilized by a salt bridge between 22Glu/23Asp and 28Lys, may nucleate folding and aggregation of the Aβ peptide. In the present paper we test this hypothesis by studying how salt bridge and turn formation vary with intrinsic and environmental changes, and how these changes effect folding and aggregation of the Aβ peptide.
摘要
淀粉样沉积物是许多疾病的一个标志。就阿尔茨海默病而言，在21位丙氨酸和30位丙氨酸之间的一个转角，由22位谷氨酸/23位天冬氨酸与28位赖氨酸之间的盐桥稳定，可能引发Aβ肽的折叠和聚集。在本文中，我们通过研究盐桥和转角的形成如何随内在和环境变化而变化，以及这些变化如何影响Aβ肽的折叠和聚集来检验这一假设。
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