| 血管紧张素转换酶与抑制肽结合模式的分子动力学研究 |
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| 引用本文： | 王嵩,管珊珊,万永凤,单亚明,张浩.血管紧张素转换酶与抑制肽结合模式的分子动力学研究[J].高等学校化学学报,2017,38(7). |
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| 作者姓名： | 王嵩 管珊珊 万永凤 单亚明 张浩 |
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| 作者单位： | 1. 吉林大学理论化学研究所理论化学计算实验室,长春,130061;2. 吉林大学理论化学研究所理论化学计算实验室, 长春 130061;吉林大学生命科学学院, 艾滋病疫苗国家工程实验室, 长春 130012;3. 吉林大学生命科学学院, 艾滋病疫苗国家工程实验室, 长春 130012 |
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| 基金项目： | 国家自然科学基金，吉林省教育厅十三五规划项目，徐州市玛泰生物科技有限公司科技攻关项目，吉林大学研究生创新基金(批准号:2016008)资助.Supported by the National Natural Science Foundation of China，the 13th Five-Year Plan of Jilin Provincial Department of Education |
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| 摘 要： | 应用分子模拟方法研究了血管紧张素转换酶(Angiotensin-converting enzyme,ACE)C端结构域(C-domain)与两种抑制肽(RIGLF/AHEPVK)的结合机制,预测了两个体系的结合模式,提出在C-domain-RIGLF中His353,Asp377,Asp453,Phe457,His513,Tyr523和Phe527为RIGLF主要结合残基,而在C-domainAHEPVK中Gln281,His353,Ser355,Glu384,Lys511,His513和Tyr523等残基起关键作用.应用结合自由能计算比较了两个体系的结合能力,结果表明,RIGLF和AHEPVK均与C-domain活性位点残基存在较强作用,且AHEPVK对C-domain的结合能力较强,与实验结果一致.
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| 关 键 词： | 血管紧张素转换酶 抑制肽 分子对接 分子动力学模拟 结合自由能计算 |
Molecular Dynamics Simulation Study on the Binding Modes of Angiotensin-converting Enzyme with Inhibitory Peptides |
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| WANG Song,GUAN Shanshan,WAN Yongfeng,SHAN Yaming,ZHANG Hao.Molecular Dynamics Simulation Study on the Binding Modes of Angiotensin-converting Enzyme with Inhibitory Peptides[J].Chemical Research In Chinese Universities,2017,38(7). |
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| Authors: | WANG Song GUAN Shanshan WAN Yongfeng SHAN Yaming ZHANG Hao |
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| Abstract: | Binding modes of C-domain of Angiotensin-converting enzyme(ACE) and two peptides RIGLF and AHEPVK which had competitive inhibited potency against ACE,C-domain-RIGLF and C-domain-AHEPVK were investigated with molecular docking,molecular dynamics simulation,and binding free energy,calculation.The calculation results indicate that vital binding residues in C-domain-RIGLF are His353,Asp377,Asp453,Phe457,His513,Tyr523 and Phe527,while key residues in C-domain-AHEPVK are Gln281,His353,Ser355,Glu384,Lys511,His513 and Tyr523.The binding ability between C-domain-RIGLF and C-domain-AHEPVK were compared via MM-PBSA calculation.The calculated results indicate that AHEPVK binds C-domain more easily than RIGLF.The result is consistent with experimental data.The results have academic guidance meaning for exploring the mechanism of how foodborne peptide inhibitors bind to ACE and this work provides the clues for novel medicines design which are mainly aimed at ACE. |
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| Keywords: | Angiotensin-converting enzyme Inhibitory peptide Molecular docking Molecular dynamics simulation Free energy calculation |
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