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Identification, characterization, and insights into the mechanism of novel dipeptidyl peptidase-IV inhibitory peptides from yak hemoglobin by in silico exploration, molecular docking, and in vitro assessment

文献类型： 外文期刊

作者： Zhang, Jin 1 ; Wu, Yulong 1 ; Tang, Honggang 1 ; Li, Huanhuan 1 ; Da, Se 3 ; Ciren, Dajie 3 ; Peng, Xinyan 4 ; Zhao, Ke 1 ;

作者机构： 1.Zhejiang Acad Agr Sci, Inst Food Sci, State Key Lab Managing Biot & Chem Threats Qual &, Hangzhou 310021, Zhejiang, Peoples R China

2.Hangzhou Normal Univ, Sch Publ Hlth, Hangzhou 311121, Zhejiang, Peoples R China

3.Gonyal Anim Husb Technol & Ind Co, Naqu 852014, Tibet, Peoples R China

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

5.Zhejiang Acad Agr Sci, Inst Food Sci, 198 Shiqiao Rd, Hangzhou 310021, Zhejiang, Peoples R China

关键词： Dipeptidyl peptidase IV; Peptide; Yak hemoglobin; Molecular docking; In silico screening; In vitro assessment

期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：7.7； 五年影响因子：7.7 ）

ISSN： 0141-8130

年卷期： 2024 年 259 卷

页码：

收录情况： SCI

摘要： Dipeptidyl peptidase IV (DPP-IV) inhibitory peptides were screened and identified from yak hemoglobin for the first time by in silico analysis, molecular docking, and in vitro evaluation. Results showed that yak hemoglobin had a high potential to produce DPP-IV inhibitory peptides based on the sequence alignment and bioactive potential evaluation. Furthermore, "pancreatic elastase + stem bromelain" was the optimal combined-enzymatic strategy by simulated proteolysis. Additionally, 25 novel peptides were found from its simulated hydrolysate, among which 10 peptides had high binding affinities with DPP-IV by molecular docking. Most of these peptides were also in silico characterized with favorable physicochemical properties and biological potentials, including relatively low molecular weight, high hydrophobicity, several net charges, good water solubility, nontoxicity, acceptable sensory quality, and good human intestinal absorption. Finally, six novel DPP-IV inhibitory peptides were identified via in vitro assessment, among which EEKA (IC50 = 235.26 mu M), DEV (IC50 = 339.45 mu M), and HCDKL (IC50 = 632.93 mu M) showed the strongest capacities. The hydrogen bonds and electrostatic attractions formed with core residues within the S2 pocket of DPP-IV could be mainly responsible for their inhibition performances. This work provided a time-saving method and broadened application for yak by-products development as sources of functional foods.

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