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.%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-domain-AHEPVK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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