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Mechanistic Study of Novel Dipeptidyl Peptidase IV Inhibitory Peptides from Goat's Milk Based on Peptidomics and In Silico Analysis

文献类型： 外文期刊

作者： Wu, Yulong 1 ; Zhang, Jin 2 ; Zhu, Ruikai 1 ; Zhang, Hong 2 ; Li, Dapeng 2 ; Li, Huanhuan 2 ; Tang, Honggang 2 ; Chen, Lihong 2 ; Peng, Xinyan 4 ; Xu, Xianrong 1 ; Zhao, Ke 2 ;

作者机构： 1.Hangzhou Normal Univ, Sch Publ Hlth, Hangzhou 311121, Peoples R China

2.Zhejiang Acad Agr Sci, Inst Food Sci, Hangzhou 310021, Peoples R China

3.Shaanxi Normal Univ, Coll Food Engn & Nutr Sci, Xian 710062, Peoples R China

4.Yantai Univ, Coll Life Sci, Yantai 264005, Peoples R China

关键词： dipeptidyl peptidase IV; inhibitory peptide; goat milk; LC-MS/MS; virtual screening; molecular docking

期刊名称：FOODS （ 影响因子：4.7； 五年影响因子：5.1 ）

ISSN：

年卷期： 2024 年 13 卷 8 期

页码：

收录情况： SCI

摘要： Two novel dipeptidyl peptidase IV (DPP-IV) inhibitory peptides (YPF and LLLP) were discovered from goat milk protein by peptidomics, in silico analysis, and in vitro assessment. A total of 698 peptides (<23 AA) were successfully identified by LC-MS/MS from goat milk hydrolysates (hydrolyzed by papaian plus proteinase K). Then, 105 potential DPP-IV inhibitory peptides were screened using PeptideRanker, the ToxinPred tool, Libdock, iDPPIV-SCM, and sequence characteristics. After ADME, physicochemical property evaluation, and a literature search, 12 candidates were efficiently selected and synthesized in vitro for functional validation. Two peptides (YPF and LLLP) were found to exert relatively high in vitro chemical system (IC50 = 368.54 +/- 12.97 mu M and 213.99 +/- 0.64 mu M) and in situ (IC50 = 159.46 +/- 17.40 mu M and 154.96 +/- 8.41 mu M) DPP-IV inhibitory capacities, and their inhibitory mechanisms were further explored by molecular docking. Our study showed that the formation of strong non-bonding interactions with the core residues from the pocket of DPP-IV (such as ARG358, PHE357, GLU205, TYR662, TYR547, and TYR666) might primarily account for the DPP-IV inhibitory activity of two identified peptides. Overall, the two novel DPP-IV inhibitory peptides rapidly identified in this study can be used as functional food ingredients for the control of diabetes.

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