文献类型：期刊文献

英文题名：In vitro-in silico screening strategy and mechanism of angiotensin I-converting enzyme inhibitory peptides from α-lactalbumin

作者：Xie, Dewei[1];Du, Lei[1];Lin, Haisheng[2];Su, Erzheng[3];Shen, Yaling[1];Xie, Jingli[1,4];Wei, Dongzhi[1,4]

机构：[1]East China Univ Sci & Technol, New World Biotechnol Inst, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[2]Guangdong Ocean Univ, Guangdong Prov Key Lab Aquat Prod Proc & Safety, Zhanjiang 524088, Peoples R China;[3]Nanjing Forestry Univ, Coll Light Ind & Food Engn, Nanjing 210037, Peoples R China;[4]Shanghai Collaborat Innovat Ctr Biomfg SCICB, Shanghai 200237, Peoples R China

年份：2022

卷号：156

外文期刊名：LWT-FOOD SCIENCE AND TECHNOLOGY

收录：;EI(收录号：20215211399773);WOS:【SCI-EXPANDED(收录号:WOS:000741388100006)】；

基金：This work was supported by National Key Research and Development Program of China (No. 2020YFA0907800); the National Natural Science Foundation of China (Grant No. 31801489); Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety (GDPKLAPPS2001), China.

语种：英文

外文关键词：ACE inhibitory peptide; Alpha-lactalbumin; Molecular docking; Structure-activity relation; Inhibitory mechanism

摘要：This work proposed an in vitro-in silico strategy for the discovery of angiotensin I-converting enzyme (ACE) inhibitory peptides. Alpha-lactalbumin was hydrolyzed by pepsin and pancreatin. The hydmlysate under 3 kDa was separated into five fractions, among which the fractions F3, F4 and F5 exhibited potent ACE inhibition, by ultrafiltration and dextran gel chromatography. Thirty-eight peptides were identified by Nano-HPLC-MS/MS from fractions F3, F4 and F5 to form a peptide library. Five novel ACE inhibitory peptides (SLPEW, VSLPEW, GVSLPEW, VGINYW and LDQWL) were predicted according to the binding energy calculated by molecular docking. The IC50 values of such peptides ranged from 6.94 to 17.5 mu mol/L. Lineweaver-Burk plots revealed LDQWL as competitive inhibitor, and SLPEW and VSLPEW as mixed-type, while other peptides as non-competitive ones. Molecular docking showed that the competitive inhibitors interacted with the residues of active pocket, and the non-competitive peptides connected to the residues outside the active site and the mixed-type inhibitors anchored in both entrance channel and active pocket of ACE. Circular dichroism indicated that these peptides significantly changed the secondary structure of ACE. VGINYW binding caused the most reduction of alpha-helix and the most increase of random coils.