文献类型：期刊文献

英文题名：Dipeptidyl peptidase IV inhibitory peptides from Chlorella vulgaris: in silico gastrointestinal hydrolysis and molecular mechanism

作者：Zhu, Qiaosha[1];Chen, Xujun[1];Wu, Junjie[1];Zhou, Yan[1];Qian, Yang[2];Fang, Ming[1];Xie, Jingli[1,3];Wei, Dongzhi[1,3]

机构：[1]East China Univ Sci & Technol, Sch Biotechnol, Dept Food Sci & Technol, State Key Lab Bioreactor Engn, 130 Meilong Rd,283, Shanghai 283, Peoples R China;[2]Fudan Univ, Zhongshan Hosp, Dept Radiotherapy, Shanghai 200032, Peoples R China;[3]SCICB, Shanghai 200237, Peoples R China

年份：2017

卷号：243

期号：10

起止页码：1739

外文期刊名：EUROPEAN FOOD RESEARCH AND TECHNOLOGY

收录：;EI(收录号：20171403517028);WOS:【SCI-EXPANDED(收录号:WOS:000410810100006)】；

基金：This work was supported by the "National Natural Science Foundation of China (No. 31301413)", "Open Funding Project of the State Key Laboratory of Bioreactor Engineering", and "National Basic Research Program of China (No. 2012CB721103)".

语种：英文

外文关键词：Chlorella vulgaris; DPP-IV inhibitory peptides; In silico hydrolysis; Molecular docking

摘要：Chlorella vulgaris: is a nutritional food with high protein content. Thus, 43 protein sequences from C. vulgaris were in silico gastrointestinal digested with the aid of BIOPEP. A peptide library of 468 di- and tri-peptides was built from the produced peptides. Six peptides, AAR, VPA, VPW, IPL, IPR, and PPL, were selected for DPP-IV inhibitory assay based on their sequence feature with Pro or Ala at the second N-terminal site. VPA, VPW, IPL, and IPR had potency of DPP-IV inhibition. VPW and IPR with the same N-terminal and second N-terminal sites as those of diprotin A (IPI) and diprotin B (VPL) achieved relative inhibitory IC50 value of 6.4 and 6.9 versus IPI. These peptides were further demonstrated gastrointestinal stable in vitro and could also inhibit the DPP-IV in mouse serum. Molecular docking illustrated the inhibitory mechanism of VPW and IPR. Both VPW and IPR binding with DPP-IV through hydrogen bonds, van Edward Mars interactions, and hydrophobic interactions. However, VPW formed more stable interaction with DPP-IV. The results suggested that C. vulgaris proteins would be a good source for DPP-IV inhibitory peptides.