文献类型：期刊文献

英文题名：Angiotensin I-converting enzyme inhibitory peptides from Sipuncula (Phascolosoma esculenta): Purification, identification, molecular docking and antihypertensive effects on spontaneously hypertensive rats

作者：Guo, Mingrong[1];Chen, Xujun[1];Wu, Yanling[1];Zhang, Lujia[1];Huang, Weixue[2];Yuan, Ying[3];Fang, Ming[1];Xie, Jingli[1,4];Wei, Dongzhi[1,4]

机构：[1]East China Univ Sci & Technol, Dept Food Sci & Engn, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[2]Chinese Acad Sci, Shanghai Inst Organ Chem, State Key Lab Bioorgan & Nat Prod Chem, Shanghai 200032, Peoples R China;[3]Shanghai Univ Tradit Chinese Med, Coll Pharm, Shanghai 201203, Peoples R China;[4]Shanghai Collaborat Innovat Ctr Biomfg, Shanghai 200237, Peoples R China

年份：2017

卷号：63

起止页码：84

外文期刊名：PROCESS BIOCHEMISTRY

收录：;EI(收录号：20173904213855);WOS:【SCI-EXPANDED(收录号:WOS:000418222500012)】；

基金：This work was supported by "National Natural Science Foundation of China" (No. 31301413 and 31571786), and "Open Funding Project of the State Key Laboratory of Bioreactor Engineering".

语种：英文

外文关键词：Phascolosoma esculenta; Angiotensin I converting enzyme inhibitory peptide; Antihypertensive activity; Spontaneously hypertensive rats

摘要：Three novel angiotensin-I converting enzyme inhibitory peptides were explored from Sipuncula (Phascolosoma esculenta), a seafood with high protein content. Peptides RYDF, YASGR and GNGSGYVSR were obtained by hydrolysis of the water-soluble protein of Sipuncula with pepsin and trypsin. The peptides were purified through gel filtration and reverse-phase high-performance liquid chromatography, and identified by de novo sequencing method of MALDI-TOF. All three peptides are non-competitive inhibitors of angiotensin-I converting enzyme determined by Lineweaver-Burk plots. Their inhibitory IC50 values were 235, 184 and 2911M, respectively. The inhibitory mechanism was well illustrated through molecular docking. The docking results showed that the differences of inhibitory activities of the three peptides were due to the degree of non-covalent bond-based interactions between the peptides and angiotensin-I converting enzyme, especially the hydrogen bonds. The antihypertensive effect of peptides was confirmed by their lowering blood pressure in spontaneously hypertensive rats with the oral administration as 5 mg/kg body weight. Peptide GNGSGYVSR decreased systolic blood pressure 31 mmHg at 2 h after oral administration, and maintained the level till 4 h. Therefore, peptides from Sipuncula can be considered as promising candidates for ACE inhibition and hypertension treatment.