Key Laboratory of Biorheological Science and Technology, Ministry of Education, Bioengineering College, Chongqing University, Chongqing 400044, China.
Chongqing Academy of Animal Sciences, Chongqing Engineering Research Center of Meat Quality Evaluation and Processing, Rongchang, Chongqing 402460, China; School of Agriculture, Jinhua Polytechnic, Jinhua, Zhejiang, Jinhua 321000, China.
Bioorg Chem. 2022 May;122:105736. doi: 10.1016/j.bioorg.2022.105736. Epub 2022 Mar 12.
Duck embryonic proteins are a promising source of food-derived functional peptides. Using a combination of experiments and bioinformatics approaches, a tri-peptide inhibitor YPW targeting iNOS was identified from duck embryo protein hydrolysates. Our results indicated that YPW could significantly inhibit LPS-induced NO generation in macrophages in a dose-dependent manner. YPW also significantly inhibited the expression of IL-6 and iNOS. Molecular simulations revealed that YPW could interact strongly with (iNOS) with a binding energy of -45.71 ± 17.75 kJ/mol. The stability of YPW-iNOS was maintained by the hydrogen bonds of amino acid residues Ile, Gly, Gly, Glu, Asn, and Trp, and the hydrophobic interactions by Trp, Phe, and Val. In conclusion, our study provides a new idea for broadening the utilization of duck embryo proteins, and a strategy for the discovery of food-derived bioactive peptides.
鸭胚胎蛋白是一种很有前途的食物来源功能性肽。本研究采用实验与生物信息学相结合的方法，从鸭胚胎蛋白水解物中鉴定出一种靶向 iNOS 的三肽抑制剂 YPW。结果表明，YPW 可剂量依赖性地显著抑制 LPS 诱导的巨噬细胞中 NO 的产生。YPW 还显著抑制了 IL-6 和 iNOS 的表达。分子模拟表明，YPW 可以与（iNOS）强烈相互作用，结合能为-45.71±17.75 kJ/mol。YPW-iNOS 的稳定性通过残基 Ile、Gly、Gly、Glu、Asn 和 Trp 的氢键和 Trp、Phe 和 Val 的疏水相互作用来维持。总之，本研究为拓宽鸭胚胎蛋白的利用提供了新思路，为发现食物来源的生物活性肽提供了策略。
