文献类型：期刊文献

中文题名：白果肽的二肽基肽酶-Ⅳ抑制活性及其抑制机理研究

英文题名：Study on dipeptidyl peptidase-Ⅳinhibitory activity and mechanism of peptides derived from Ginkgo biloba seeds

作者：王翔[1] 张彩虹[1] 蒋建新[2] 谢普军[1] 黄立新[1]

第一作者：王翔

机构：[1]中国林业科学研究院林产化学工业研究所,江苏南京210042;[2]北京林业大学材料科学与技术学院,北京100083

年份：2024

卷号：50

期号：6

起止页码：109-115

中文期刊名：食品与发酵工业

外文期刊名：Food and Fermentation Industries

收录：CSTPCD;;EI(收录号：20253719143963);Scopus;北大核心:【北大核心2023】；CSCD:【CSCD2023_2024】；

基金：江苏省农业科技创新基金(CX(22)3056)。

语种：中文

中文关键词：二肽基肽酶-Ⅳ;抑制机理;白果肽;分子对接;分子动力学模拟

外文关键词：dipeptidyl peptidaseⅣ;inhibition mechanism;peptides derived from Ginkgo biloba seeds;molecular docking;molecular dynamics simulation

分类号：TS201.2

摘要：食源性二肽基肽酶-Ⅳ(dipeptidyl peptidaseⅣ,DPP-Ⅳ)抑制肽可有效调节机体内糖代谢,降低机体血糖水平。为评估白果肽(phenylalanine-alanine-proline-serine-tryptophan,FAPSW和methionine-proline-glycine-proline-proline,MPGPP)的降糖潜能,采用体外试验测定其DPP-Ⅳ抑制活性,并进一步通过分子对接和分子动力学模拟揭示其抑制机理。结果表明,FAPSW和MPGPP具有良好的DPP-Ⅳ抑制活性,且MPGPP的DPP-Ⅳ抑制活性[IC_(50)=(0.158±0.009)g/L]强于FAPSW[IC_(50)=(2.540±0.126)g/L];分子对接结果表明,静电相互作用、氢键、疏水作用和范德华力在FAPSW和MPGPP抑制DPP-Ⅳ活性中起重要作用;分子动力学结果表明,FAPSW和MPGPP结合DPP-Ⅳ能形成稳定的复合物结构,且MPGPP-DPP-Ⅳ复合物的稳定性要强于FAPSW-DPP-Ⅳ。结合自由能结果表明,静电相互作用在FAPSW和MPGPP结合DPP-Ⅳ中起主导作用。研究结果可为FAPSW和MPGPP在功能食品领域的开发和利用提供一定的理论参考。
The food-derived dipeptidyl peptidaseⅣ(DPP-Ⅳ)inhibitory peptides can effectively modulate glucose metabolism and reduced blood glucose levels in the body.To evaluate the potential hypoglycemic effects of two peptides(phenylalanine-alanine-proline-serine-tryptophan,FAPSW and methionine-proline-glycine-proline-proline,MPGPP),their DPP-Ⅳinhibitory activity was determined by in vitro inhibition experiments.Molecular docking and molecular dynamics simulation were performed to further revealed their inhibition mechanisms.Results showed that both FAPSW and MPGPP had good DPP-Ⅳinhibitory activity and the DPP-Ⅳinhibitory activity of MPGPP[IC_(50)=(0.158±0.009)g/L]was stronger than that of FAPSW[IC_(50)=(2.540±0.126)g/L].Molecular docking results suggested that electrostatic interactions,hydrogen bonds,hydrophobic interactions,and van der Waals forces played important roles in the DPP-Ⅳinhibition activity of FAPSW and MPGPP.Molecular dynamics simulation results showed that FAPSW and MPGPP could form stable complexes by binding to DPP-Ⅳ,and the MPGPP-DPP-Ⅳcomplex exhibited stronger stability compared to the FAPSW-DPP-Ⅳcomplex.The binding free energy results indicated that electrostatic interactions contributed to the binding of FAPSW and MPGPP with DPP-Ⅳ.These findings provide a theoretical reference for the development and utilization of FAPSW and MPGPP in the field of functional foods.