Rapid Screening and Verification of α-Lactalbumin-Derived ACE Inhibitory Peptides

被引：1

作者：

Hou C. ^{[1
]}

Nie C. ^{[1
]}

Wang Y. ^{[1
]}

Ai L. ^{[1
]}

Xia Y. ^{[1
]}

Zhang H. ^{[1
]}

Xie F. ^{[1
]}

Wang G. ^{[1
]}

机构：

[1] School of Medical Instrument and Food Engineering, University of Shanghai for Science and Technology, Shanghai

来源：

Shipin Kexue/Food Science | 2021年 / 42卷 / 24期

关键词：

Angiotensin I-converting enzyme inhibitory peptide; Molecular docking; Virtual screening; α-lactalbumin;

D O I：

10.7506/spkx1002-6630-20201012-094

中图分类号：

学科分类号：

摘要：

In our present study, virtual enzymatic hydrolysis of α-lactalbumin was investigated using online bioinformatic tools. The activity, toxicity, and physicochemical properties of the resulting bioactive peptides were predicted. A novel angiotensin I-converting enzyme (ACE) inhibitory peptide, Pro-Glu-Trp (PEW), was selected by molecular docking. PEW was synthesized by the solid phase method and its activity was verified in vitro, showing a half-maximal inhibitory concentration (IC50) value of 3 130 μmol/L. The molecular docking simulation results showed that the interaction between PEW and ACE's active-site pocket S1 may be the major reason for its ACE inhibitory activity. Hydrogen bonding,hydrophobic force, and electrostatic force were the major forces maintaining their mutual binding. Compared with traditional methods, the protocol presented in this study could quickly and efficiently screen ACE inhibitory peptides, which may provide a new idea for the rapid screening of food-derived bioactive peptides. © 2021, China Food Publishing Company. All right reserved.

引用

页码：100 / 107

页数：7

共 37 条

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