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Identification and In Silico Characterization of the Novel Inhibitory Peptides of Angiotensin Converting Enzyme from Donkey Meat

文献类型： 外文期刊

作者： Deng, Zixin 1 ; Li, Mingyu 1 ; Zhang, Zeyu 1 ; Chen, Chao 1 ; Qu, Xia 1 ; Wang, Zhenyu 1 ; Zhang, Dequan 1 ; Zhang, Chunjiang 1 ; Wu, Boxian 3 ; Sang, Xueyu 3 ;

作者机构： 1.Chinese Acad Agr Sci CAAS, Minist Agr & Rural Affairs, Inst Food Sci & Technol, Integrated Lab Proc Technol Chinese Meat Dishes, Beijing 100193, Peoples R China

2.Chinese Acad Agr Sci, Chengdu Natl Agr Sci & Technol Ctr, Inst Urban Agr, Chengdu 610213, Peoples R China

3.Shandong Donge Black Donkey Anim Husb Technol Co L, Liaocheng 252000, Shandong, Peoples R China

关键词： Donkey meat; Angiotensin converting enzyme inhibitory activity; Active peptides; Molecular docking; In Silico proteolysis

期刊名称：INTERNATIONAL JOURNAL OF PEPTIDE RESEARCH AND THERAPEUTICS （ 影响因子：2.4； 五年影响因子：2.0 ）

ISSN： 1573-3149

年卷期： 2025 年 31 卷 2 期

页码：

收录情况： SCI

摘要： Propose Present study identified the peptides with ACE inhibitory activity from donkey meat hydrolysates. Method Donkey meat hydrolysates were prepared by enzymatic hydrolysis (pepsin and trypsin). Hydrolysates of different molecular weights (Mw) were analyzed for their activity and composition, and peptides were identified by Nano-LC-MS/MS. The identified peptides were screened by bioinformatics and molecular docking, and the potential ACE inhibitory peptides were selected for synthesis to verify their activity. Results The results showed that the percentage of peptides with a Mw of < 1000 Da was as high as 80.71%, and the F1 (< 1000 Da) fraction had the highest content of non-hydrophobic amino acids (42.72%). F1 had the highest ACE inhibitory activity, with 66.76 +/- 1.43% inhibition at a concentration of 2 mg/mL. Identification and screening results of F1 showed that AAIFPGGF, VGPAPWGF, LPFL, APFL, and APFF had a good affinity with ACE. Molecular docking results indicated that the peptide VGPAPWGF exhibited a strong binding affinity, with a binding energy of -93.45 kcal/mol. VGPAPWGF formed hydrogen bonds predominantly with key amino acid residues located in the S1 and S2' active pockets of the target enzyme. Enzymatic resistance studies have demonstrated that VGPAPWGF exhibits resistance to both pepsin and trypsin, indicating that the peptide is relatively stable throughout the digestive process. Conclusion VGPAPWGF had the strongest ACE inhibitory activity and binding affinity for the ACE active sites, and it exhibited resistance to enzymatic degradation. Therefore, VGPAPWGF from donkey meat could be utilized in the development of functional food components for the prevention of hypertension.

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