4种食源性三肽lRP（ lle-Arg-Pro），lKP（ lle-Lys-Pro），GRP（ Gly-Arg-Pro），lRA（ lle-Arg-Ala）的ACE抑制活性已得到实验证实，但其与ACE的相互作用模式与分子机制尚不清楚，本研究采用柔性分子对接方法解决这一问题。分子对接结果表明：4种三肽与ACE有相似的作用模式，氢键、亲水、疏水、静电等作用力共同对三肽与 ACE 的结合存在贡献，但以氢键作用为主；ACE 分子中 Lys511，His513， Tyr520，Tyr523等氨基酸残基为其与肽结合的重要结合位点；ACE抑制三肽中氮端氨基和碳端羧基对其抑制活性影响显著，其中氮端氨基的作用更为重要。通过以上分子机理研究可为开发强活性ACE抑制肽提供理论指导。%The ACE inhibitory activities of four food-derived tripeptides,including lRP,lKP,GRP and lRA,were verified by some experiments. However,their interaction modes with ACE and mo-lecular mechanism remain unclear. This research focused on resolving the above problems using flexi-ble molecular docking method. The molecular docking results demonstrated that four peptides had similar action modes with ACE. Hydrogen bond,hydrophilic,hydrophobic and electrostatic interac-tions were together responsible for the conformational stability of the complexes formed by peptides and ACE,in which hydrogen bond was the most important interaction. Amino acid residues Lys511, His513,Tyr520,Tyr523 in ACE molecule were the most important binding sites combined with ac-tive peptides. N-terminal amino groups and C-terminal carboxyl of ACE inhibitory peptides were the key groups for the activities of tripeptides,especially the N-terminal amino groups. The above infor-mation will be helpful for the development of ACE inhibitory peptides with high activities.
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