结合分子对接技术研究牦牛乳干酪苦味肽RK7和KQ7的α-淀粉酶抑制活性  

Using Molecular Docking to Investigate the Alpha-amylase Inhibitory Activity of Bitter Peptides RK7 and KQ7 Derived from Yak Cheese

作　　者：李梦瑶 梁琪[1,2] 宋雪梅 LI Mengyao;LIANG Qi;SONG Xuemei(College of Food Science and Engineering,Gansu Agricultural University,Lanzhou 730070,China;Functional Dairy Product Engineering Laboratory of Gansu,Lanzhou 730070,China)

机构地区：[1]甘肃农业大学食品科学与工程学院,甘肃兰州730070 [2]甘肃省功能乳品工程实验室,甘肃兰州730070

出　　处：《食品科学》2023年第2期132-138,共7页Food Science

基　　金：国家自然科学基金地区科学基金项目(31660468)。

摘　　要：以牦牛乳干酪苦味肽RPKHPIK(RK7)和KVLPVPQ(KQ7)为研究对象,通过生物信息学方法,使用ExPASy-ProtParam、Innovagen和PepDraw等工具计算RK7和KQ7的理化性质,利用分子对接技术揭示抑制α-淀粉酶的作用机制,结合体外实验测定α-淀粉酶抑制活性。研究表明:RK7和KQ7的分子质量分别为875.07 Da和779.98 Da,疏水性分别为42.86%和71.42%;分子对接显示α-淀粉酶中的His305、Glu233、Trp59和Trp58与RK7和KQ7的结合起重要作用,并且Asp197、Glu233和Asp300是影响α-淀粉酶活性的关键氨基酸;体外活性验证发现,RK7和KQ7α-淀粉酶的IC50分别为0.45 mg/mL和0.86 mg/mL。本研究通过生物信息学方法结合体外活性实验,高效快速获得牦牛乳源α-淀粉酶抑制肽,并通过分子对接技术探究分子间的作用机制,为α-淀粉酶抑制肽的研究提供新思路。In this study,the physicochemical properties of two bitter peptides derived from yak cheese,RPKHPIK(RK7)and KVLPVPQ(KQ7)were calculated by using online bioinformatics tools such as ExPASy-ProtParam,Innovagen,and Pep-Draw.Molecular docking was used to elucidate the mechanism of the inhibitory effect of the two peptides onα-amylase and theirα-amylase inhibitory activity was determined.The results showed that the molecular masses of RK7 and KQ7 were 875.07 and 779.98 Da,and their hydrophobicity were 42.86%and 71.42%,respectively.Molecular docking showed that His305,Glu233,Trp59 and Trp58 inα-amylase played an important role in binding to RK7 and KQ7.Furthermore,Asp197,Glu233 and Asp300 were the key amino acids for the activity ofα-amylase.The half maximal inhibitory concentration(IC50)of RK7 and KQ7 againstα-amylase were 0.45 and 0.86 mg/mL,respectively.The findings of this study provide new evidence for the study ofα-amylase inhibitory peptides.

关 键 词：牦牛乳干酪 苦味肽 α-淀粉酶抑制活性 分子对接 作用机制 

分 类 号：TS252.5[轻工技术与工程—农产品加工及贮藏工程]