Identification of two novel dipeptidyl peptidase-IV inhibitory peptides from sheep whey protein and inhibition mechanism revealed by molecular docking  

作　　者：Xinge Zhang Rongchun Wang Cuilin Cheng Yingchun Zhang Ying Ma Weihong Lu 

机构地区：[1]Department of Food Nutrition and Health,School of Medicine and Health,Harbin Institute of Technology,Harbin,150001,China [2]Zhengzhou Institute,Harbin Institute of Technology,Zhengzhou,450001,China

出　　处：《Food Bioscience》2022年第4期145-152,共8页食品生物科学（英文）

基　　金：supported by Science and Technology Planning Project of Sichuan Province(2022JDRC0039 and 2021YFSY0035).

摘　　要：In this study,the peptides with dipeptidyl peptidase-IV(DPP-IV)inhibitory activities were obtained by trypsin hydrolysis from sheep whey protein.The results showed that the highest DPP-IV inhibitory activity of the hydrolysate(77.80%±1.87%)was obtained by trypsin enzymolysis for 4.0 h with 24.50%±0.05%of the degree of hydrolysis(DH).Peptides with inhibitory activity against DPP-IV were purified using anion-exchange(DEAE-52)and size-exclusion(G15 dextran gel)chromatography.A total of 86 peptides were identified using LC-MS/MS.The binding energies of RLYLHENK(RL8)and MQEHFTCCR(MQ9)to DPP-IV were determined to be-11.29 kcal/mol and-10.79 kcal/mol with molecular docking in silico,respectively.RL8 and MQ9 could bind to DPP-IV mainly through hydrogen bonds and hydrophobic interactions,and inhibit the DPP-IV enzyme by occupying the S2 pocket.The IC50 values of RL8 and MQ9 in vitro were 166.4μmol/L and 214.8μmol/L,respectively.The inhibitory activities in situ modes of the two peptides were evaluated using Caco-2 cells.The IC50 values of RL8 and MQ9 in situ were 158.3μmol/L and 251.6μmol/L,respectively.The RL8 and MQ9 derived from sheep whey protein can be considered as a potential source of natural DPP-IV inhibitor.

关 键 词：DPP-IV inhibitory activity Bioactive peptide Sheep whey protein Molecular docking Inhibition mechanism 

分 类 号：TS201[轻工技术与工程—食品科学]