老年痴呆相关蛋白靶标结构与功能关系的分子动力学模拟_英文_许叶春.pdfVIP

26 2 Vol.26 No.2 2009 3 Journal of the Graduate School of the Chinese Academy of Sciences March　2009 Article ID:1002-117 (2009)02-0280-08 EXCERPT OF DISSERTATION Molecular dynamics simulations studies on the structure-function relationship of protein tar ets related to Alzheimers disease XU Ye-Chun 　JIANG Hua-Liang (Drug D iscovery and Design Center, State Key Laboratory of Drug Research, Shanghai I nstitute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China ) (Received 2 April 2008) Xu YC, Jian HL.Molecular dynamics simulations studies on the structure-function relationship of protein tar ets related to Alzheimer s disease.J ournal of the Graduate School of the Chinese Academy of Sciences, 2009, 26(2):280～ 287 Abstract 　In the present thesis, the conformational changes of β-amyloid peptide, the dynamic binding and unbinding processes of huperzine A to acetylcholinesterase, and the conformational movement associated with the open or close gating mechanism of nicotinic acetylcholine receptor have been investigated using conventional and or steered molecular dynamics simulations, gaining new and useful insights for the pathogenetic mechanism of Alzheimer s disease (AD), and providing new clues for discovering new anti-AD drugs. Key words　Alzheimers disease, molecular dynamics simulation, β-amyloid peptide, acetylcholines- terase huperzine A, nicotinic acetylcholine receptor CLC　R962 1　Introduction Alzheimer s disease (AD), a progressive neurodegenerative disorder, is characterized pathologically by accumulation of t