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题名: Free energy profiles of cocaine esterase-cocaine binding process by molecular dynamics and potential of mean force simulations
作者: Zhang, Yuxin1, 2, 3;  Huang, Xiaoqin2;  Han, Keli1;  Zheng, Fang2, 3;  Zhan, Chang-Guo2, 3
关键词: Esterase ;  Cocaine ;  Binding process ;  Energy barrier
刊名: CHEMICO-BIOLOGICAL INTERACTIONS
发表日期: 2016-11-25
DOI: 10.1016/j.cbi.2016.05.011
卷: 259, 页:142-147
收录类别: SCI ;  ISTP
文章类型: Article
WOS标题词: Science & Technology ;  Life Sciences & Biomedicine
类目[WOS]: Biochemistry & Molecular Biology ;  Pharmacology & Pharmacy ;  Toxicology
英文摘要: The combined molecular dynamics (MD) and potential of mean force (PMF) simulations have been performed to determine the free energy profile of the CocE)-(+)-cocaine binding process in comparison with that of the corresponding CocE-(-)-cocaine binding process. According to the MD simulations, the equilibrium CocE-(+)-cocaine binding mode is similar to the CocE-(-)-cocaine binding mode. However, based on the simulated free energy profiles, a significant free energy barrier (similar to 5 kcal/mol) exists in the CocE-(+)-cocaine binding process whereas no obvious free energy barrier exists in the CocE-(-)-cocaine binding process, although the free energy barrier of similar to 5 kcal/mol is not high enough to really slow down the CocE-(+)-cocaine binding process. In addition, the obtained free energy profiles also demonstrate that (+)-cocaine and (-)-cocaine have very close binding free energies with CocE, with a negligible difference (similar to 0.2 kcal/mol), which is qualitatively consistent with the nearly same experimental K-M values of the CocE enzyme for (+)-cocaine and (-)-cocaine. The consistency between the computational results and available experimental data suggests that the mechanistic insights obtained from this study are reasonable. (C) 2016 Elsevier Ireland Ltd. All rights reserved.
关键词[WOS]: HIGH-ACTIVITY MUTANTS ;  BUTYRYLCHOLINESTERASE-CATALYZED HYDROLYSIS ;  FUNDAMENTAL REACTION-MECHANISM ;  PARTICLE-MESH EWALD ;  TRANSITION-STATES ;  PERTURBATION SIMULATION ;  (-)-COCAINE HYDROLYSIS ;  COMPUTATIONAL DESIGN ;  REACTION PATHWAY ;  HYDROLASE
语种: 英语
WOS记录号: WOS:000388843500014
Citation statistics: 
内容类型: 期刊论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/150421
Appears in Collections:中国科学院大连化学物理研究所_期刊论文

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作者单位: 1.Chinese Acad Sci, State Key Lab Mol React Dynam, Dalian Inst Chem Phys, Zhongshan Rd 457, Dalian 116023, Peoples R China
2.Univ Kentucky, Coll Pharm, Mol Modeling & Biopharmaceut Ctr, 789 South Limestone St, Lexington, KY 40536 USA
3.Univ Kentucky, Coll Pharm, Dept Pharmaceut Sci, 789 South Limestone St, Lexington, KY 40536 USA

Recommended Citation:
Zhang, Yuxin,Huang, Xiaoqin,Han, Keli,et al. Free energy profiles of cocaine esterase-cocaine binding process by molecular dynamics and potential of mean force simulations[J]. CHEMICO-BIOLOGICAL INTERACTIONS,2016,259:142-147.
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