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

Autor: Yulong Wu, Jin Zhang, Ruikai Zhu, Hong Zhang, Dapeng Li, Huanhuan Li, Honggang Tang, Lihong Chen, Xinyan Peng, Xianrong Xu, Ke Zhao
Jazyk: angličtina
Rok vydání: 2024
Předmět:
Zdroj: Foods, Vol 13, Iss 8, p 1194 (2024)
Druh dokumentu: article
ISSN: 2304-8158
DOI: 10.3390/foods13081194
Popis: 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 (50 = 368.54 ± 12.97 μM and 213.99 ± 0.64 μM) and in situ (IC50 = 159.46 ± 17.40 μM and 154.96 ± 8.41 μM) 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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