文献类型：期刊文献

英文题名：Comparison of an angiotensin-I-converting enzyme inhibitory peptide from tilapia (Oreochromis niloticus) with captopril: inhibition kinetics, in vivo effect, simulated gastrointestinal digestion and a molecular docking study

作者：Chen, Jiali[1];Ryu, Bomi[2];Zhang, YuanYuan[1];Liang, Peng[1];Li, Chengyong[3,4];Zhou, Chunxia[1];Yang, Ping[1];Hong, Pengzhi[1];Qian, Zhong-Ji[3,4]

机构：[1]Guangdong Ocean Univ, Coll Food Sci & Technol, Zhanjiang 524088, Peoples R China;[2]Jeju Natl Univ, Dept Marine Life Sci, Jeju, South Korea;[3]Guangdong Ocean Univ, Sch Chem & Environm Sci, Zhanjiang 524088, Peoples R China;[4]Guangdong Ocean Univ, Shenzhen Inst, Shenzhen, Peoples R China

年份：2020

卷号：100

期号：1

起止页码：315

外文期刊名：JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE

收录：SCI-EXPANDED(收录号：WOS:000494865300001)、、WOS

基金：The study was supported by the Yangfan Scarce Top Talent Project of Guangdong Province (201433009) and the Program for Scientific Research Start-Up Funds of Guangdong Ocean University (to Zhong-Ji Qian). In addition, the study was supported by Development Project about Marine Economy Demonstration of Zhanjiang City (2017C8B1). And supported by the Fund of Southern Marine Science and Engineering Guangdong Laboratory (Zhanjiang, ZJW-2019-XX)

语种：英文

外文关键词：angiotensin-I-converting enzyme; bioactive peptide; captopril; molecular docking; SHRs

外文摘要：BACKGROUND In order to utilize tilapia skin gelatin hydrolysate protein, which is normally discarded as industrial waste in the process of fish manufacture, we study the in vivo and in vitro angiotensin-I-converting enzyme (ACE) inhibitory activity of the peptide Leu-Ser-Gly-Tyr-Gly-Pro (LSGYGP). The aim was to provide a pharmacological basis of the development of minimal side effects of ACE inhibitors by comparative analysis with captopril in molecular docking. RESULTS This peptide from protein-rich wastes showed excellent ACE inhibitory activity (IC50 = 2.577 mu mol L-1) and exhibited a mixed noncompetitive inhibitory pattern with Lineweaver-Burk plots. Furthermore, LSGYGP and captopril groups both showed significant decreases in blood pressure after 6 h and maintained good digestive stability over 4 h. Molecular bond interactions differentiate competitive captopril upon hydrogen bond interactions and Zn(II) interaction. The C-terminal Pro generates three interactions (hydrogen bonds, hydrophilic interactions and Van der Waals interactions) in the peptide and effectively interacts with the S1 and S2 pockets of ACE. CONCLUSION LSGYGP, with an IC50 value of 2.577 mu mol L-1, has an antihypertensive effect in spontaneously hypertensive rats. Through comparison with captopril, this study revealed that LSGYGP may be a potential food-derived ACE inhibitory peptide and could act as a functional food ingredient to prevent hypertension. (c) 2019 Society of Chemical Industry