淀粉样β蛋白质构象转换及其抑制的分子动力学模拟  

Conformational transition of amyloid β-protein and its inhibition explored by molecular dynamics simulation

作　　者：李丽 刘夫锋 LI Li;LIU Fufeng(College of Marine and Environmental Science,Tianjin University of Science&;Technology,Tianjin 300457,China;State Key Laboratory of Food Nutrition and Safety,College of Biotechnology,Tianjin University of Science&;Technology,Tianjin 300457,China)

机构地区：[1]天津科技大学海洋与环境学院,天津300457 [2]天津科技大学生物工程学院省部共建食品营养与安全国家重点实验室,天津300457

出　　处：《生物加工过程》2019年第1期44-52,共9页Chinese Journal of Bioprocess Engineering

基　　金：国家自然科学基金(21576199;21878234);天津市自然科学基金(18JCZDJC33000);天津科技大学青年教师创新基金(2016LG17);天津科技大学大学生实验室创新基金(1705A301)

摘　　要：阿尔茨海默病(AD)是多发于老年人的神经退行性疾病。淀粉样β蛋白质(Aβ)的错误折叠和聚集与AD的发生与发展密切相关。以Aβ的错误折叠和聚集为靶标进行AD防治药物研究已成为近年来AD研究领域的热点之一。从初始的α-螺旋结构或无规卷曲构象转换形成富含β-折叠结构是Aβ聚集的关键步骤。本文中,笔者综述利用分子动力学(MD)模拟研究Aβ构象转换的分子机制,介绍MD模拟在小分子和多肽抑制剂抑制Aβ构象转换中的应用。Alzheimer′s disease(AD)is the general neurodegenerative disease in the elderly.The misfolding and the subsequent aggregation of amyloid-βprotein(Aβ)is closely related to the onset and progression of AD.The role of the misfolding and aggregation of Aβin the development of AD has been a study focus now.The conformational transition from its initialα-helix or random coil intoβ-sheet plays an important role in Aβfibrillogenesis.Here,we review the current research status on the molecular insight into the conformational transition of Aβand the inhibition mechanism of small molecular and peptide inhibitors revealed by molecular dynamics(MD)simulations.

关 键 词：淀粉样β蛋白质 构象转换 分子动力学 肽抑制剂 神经退行性疾病 

分 类 号：O641[理学—物理化学] Q51[理学—化学]