淀粉样蛋白Aβ(16-21)在水溶液中的二级结构特性研究  

Secondary Structure of Amyloid β-peptide(16-21) in Aqueous Solution

作　　者：严思仪 庄丹玲 刘佳[1,2] 杜芬芬[1,2] 蔡开聪[1,2] 

机构地区：[1]福建师范大学化学与化工学院,福建福州350007 [2]福建省理论与计算化学重点实验室,福建厦门361005

出　　处：《福建师范大学学报（自然科学版）》2015年第3期71-75,共5页Journal of Fujian Normal University：Natural Science Edition

基　　金：国家自然科学基金资助项目(21103021);福建省教育厅面上项目(JB12005);福建省教育厅高校杰出青年科研人才培育计划(JA13063);福建师范大学优秀青年骨干教师培养基金资助项目(fjsdjk2012066)

摘　　要：蛋白质的二级结构与其功能密切相关,错误的折叠将导致蛋白质生理功能的改变,甚至引起病变.以阿尔兹海默症的致病因子——淀粉样蛋白片段Aβ(16-21)为研究对象,开展分子动力学模拟,得到了Aβ(16-21)在水溶液中的全原子运动轨迹.统计结果表明,在纳秒的时间尺度上,水溶液中多肽链倾向于形成β和PPⅡ构型,进而易发生聚集,产生神经毒性.The function of protein is closely related to their secondary structure. Misfolding of the protein would cause malfunction, and even lead to disease. Molecular dynamics simulations were performed for Aβ（ 16-21 ） which is the pathogenic factor of Alzheimer＇s disease in aqueous solution. The all atom trajectories were obtained for statistical analysis. Results show that Aβ（ 16-21 ） tends to form fl and PPII conformations in aqueous solution during conformers could easily aggregate and yield neurotoxic effect. nanosecond time scale, and these

关 键 词：阿尔兹海默症 Β-淀粉样蛋白 多肽二级结构 分子动力学模拟 

分 类 号：O64[理学—物理化学]