血管紧张素转化酶抑制二肽抑制ACE作用的柔性分子对接  

Flexible Molecular Docking of Interaction between Angiotensin Ⅰ-Converting Enzyme(ACE) Inhibitory Dipeptides and ACE

作　　者：管骁[1] 刘静[2] 苏淅娜[1] 韩飞[3] 王文高 申瑞玲[6] 李景军[7] 廖丽丽 

机构地区：[1]上海理工大学医疗器械与食品学院,上海200093 [2]上海海事大学信息工程学院,上海200135 [3]国家粮食局科学研究院,北京100037 [4]上海良友(集团)有限公司,上海200333 [5]上海市粮食科学研究所,上海200333 [6]郑州轻工业学院食品与生物工程学院,河南郑州450002 [7]江苏长寿集团股份有限公司,江苏如皋226500 [8]桂林西麦食品集团,广西桂林541004

出　　处：《食品科学》2015年第5期1-6,共6页Food Science

基　　金：国家自然科学基金青年科学基金项目(31101348);上海市自然科学基金项目(14ZR1419200)

摘　　要：食源性血管紧张素转化酶(angiotensinⅠ-converting enzyme,ACE)抑制肽可有效抑制生物体内ACE活性,进而起到降压疗效,且作用温和,无副作用,是高血压治疗的理想药物,但其分子作用机制一直未有明确解释。本实验选取4个代表性食源ACE抑制二肽(Gly—Phe、Gly—Tyr、Val—Phe、Ile—Tyr)为研究对象,采用柔性分子对接的方法研究它们与ACE的相互作用模型与分子机理。分子对接结果表明:氢键、亲水、疏水、静电等作用力同时对二肽与ACE的结合有贡献,但以氢键作用为主;ACE分子中Ala354、Glu384、Arg522等氨基酸残基为二肽与其结合的重要活性位点;ACE抑制二肽中氮端氨基对其抑制活性影响显著。通过以上分子机理研究可为指导开发强活性ACE抑制肽提供理论指导。AngiotensinⅠ-converting enzyme(ACE) inhibitory peptides are ideal anti-hypertension drugs because they can inhibit ACE activity in vivo effectively,and have strong blood-reducing activity without side effects.However,their molecular mechanism remains unclear so far.In this paper,four typical ACE inhibitory dipeptides including GF(Gly-Phe),GY(Gly-Tyr),VF(Val-Phe) and IY(Ile-Tyr) were chosen as re search targets,and their action modes and molecular mechanisms on ACE were studied in detail by flexible molecular docking method.The results showed that hydrogen bond,hydrophobic,hydrophilic and electrostatic interactions existed between peptides and ACE,in which hydrogen bond interaction plays the dominant role.Moreover,Ala354,Glu384 and Arg522 in ACE were especially important binding site with active peptides,and N-terminal amino groups were the key groups in dipeptides.This information will be helpful for the molecule design of new ACE inhibitory peptides with strong activity.

关 键 词：血管紧张素转化酶 抑制二肽 分子对接 分子机理 

分 类 号：TS201.25[轻工技术与工程—食品科学]