A screening strategy for bioactive peptides from enzymolysis extracts of Lentinula edodes based on molecular docking and molecular dynamics simulation

作者：Daoyou Chen, Shen XueXiang, Wanchao Chen, Di Wu, Zhong Zhang, Peng Liu, Yanfang Liu, Wen Li, Yan Yang · 发表于：Journal of Future Foods · 年份：2024 · DOI：10.1016/j.jfutfo.2024.07.017 · 被引用次数：20 · 研究领域：Protein Hydrolysis and Bioactive Peptides、Insect Utilization and Effects、Phytochemical compounds biological activities

1. The 15 potential ACE and DPP-IV inhibitory peptides were virtually screened from 272 L. edodes flavor peptides by online prediction tools. 2. The ACE's Glu403, Glu411, Arg124, His387 and DPP-IV's Glu206, Arg125, Lys554, Asp545, Arg560 might play a key role in binding to potential bioactive peptides. 3. DAPLPHPNR and GSEDPLPGAK showed stronger binding capabilities and can formed stable complexes with the ACE and DPP-IV. 4. DAPLPHPNR and GSEDPLPGAK have strong inhibitory activity of ACE and DPP-IV, and also have certain antioxidant capacity. The aim of this study was to quickly discover multifunctional bioactive flavor peptides from the enzymolysis extracts of Lentinula edodes through bioinformatics, molecular docking and molecular dynamics simulation, and to evaluate the synthesized and in vitro activity of the screened peptides. The biological activity, toxicity, allergenicity, solubility and stability of 272 L. edodes enzymolysis flavor peptides were predicted, and 15 potential bioactive peptides were screened. By molecular docking prediction of 15 potential bioactive peptides, it was found that angiotensin-converting enzyme (ACE)'s Glu403, Glu411, Arg124, His387 and dipeptidyl peptidase IV (DPP-IV)'s Glu206, Arg125, Lys554, Asp545, Arg560 might play a key role in binding to potential bioactive peptides. Among them, DAPLPHPNR and GSEDPLPGAK showed stronger bonding energy, and the stability of their complexes was further verified by molecular dynamics simulation. In additi...