文献类型：期刊文献

英文题名：Antihypertensive Effects, Molecular Docking Study, and Isothermal Titration Calorimetry Assay of Angiotensin I-Converting Enzyme Inhibitory Peptides from Chlorella vulgaris

作者：Xie, Jingli[1,4];Chen, Xujun[1];Wu, Junjie[1];Zhang, Yanyan[3];Zhou, Yan[1];Zhang, Lujia[1];Tang, Ya-Jie[2];Wei, Dongzhi[1,4]

机构：[1]East China Univ Sci & Technol, Sch Biotechnol, Dept Food Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[2]Hubei Univ Technol, Hubei Key Lab Ind Microbiol, Hubei Prov Cooperat Innovat Ctr Ind Fermentat, Key Lab Fermentat Engn,Minist Educ, Wuhan 430068, Hubei, Peoples R China;[3]Shanghai Business Sch, Dept Food Sci, Shanghai 200235, Peoples R China;[4]SCICB, Shanghai 200237, Peoples R China

年份：2018

卷号：66

期号：6

起止页码：1359

外文期刊名：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY

收录：;EI(收录号：20180704809782);WOS:【SCI-EXPANDED(收录号:WOS:000425474000008)】；

基金：This work was supported by the National Natural Science Foundation of China (No. 31301413, 31772007), Open Funding Project of Key Laboratory of Fermentation Engineering (Ministry of Education) of China, and the Opening Project of Shanghai Key Laboratory of New Drug Design (Grant No. 17DZ2271000), China.

语种：英文

外文关键词：Chlorella vulgaris; ACE inhibitory peptides; anti hypertensive activity; molecular docking; isothermal titration calorimetry

摘要：The aim of this work is to explore angiotensin I-converting enzyme (ACE) inhibitory peptides from Chlorella vulgaris (C. vulgaris) and discover the inhibitory mechanism of the peptides. After C. vulgaris proteins were gastrointestinal digested in silico, several ACE inhibitory peptides with C-terminal tryptophan were screened. Among them, two novel noncompetitive ACE inhibitors, Thr-Thr-Trp (TTW) and Val-His-Trp (VHW), exhibited the highest inhibitory activity indicated by IC50 values 0.61 +/- 0.12 and 0.91 +/- 0.31 mu M, respectively. Both the peptides were demonstrated stable against gastrointestinal digestion and ACE hydrolysis. The peptides were administrated to spontaneously hypertensive rats (SHRs) in the dose 5 mg/kg body weight, and VHW could decrease 50 mmHg systolic blood pressure of SHRs (p < 0.05). Molecular docking displayed that both TTW and VHW formed six hydrogen bonds with active site pockets of ACE. Besides, isothermal. titration calorimetry assay discovered that VHW could form more stable complex with ACE than TTW. Therefore, VHW was an excellent ACE inhibitor.