College of Food Science and Engineering, National Engineering Laboratory of Wheat and Corn Deep Processing, Jilin Agricultural University, Changchun 130118, Jilin, China.
College of Food Science and Engineering, National Engineering Laboratory of Wheat and Corn Deep Processing, Jilin Agricultural University, Changchun 130118, Jilin, China.
Int J Biol Macromol. 2024 May;268(Pt 2):131901. doi: 10.1016/j.ijbiomac.2024.131901. Epub 2024 Apr 26.
Food-derived peptides with low molecular weight, high bioavailability, and good absorptivity have been exploited as angiotensin-converting enzyme (ACE) inhibitors. In the present study, in-vitro inhibition kinetics of peanut peptides, in silico screening, validation of ACE inhibitory activity, molecular dynamics (MD) simulations, and HUVEC cells were performed to systematically identify the inhibitory mechanism of ACE interacting with peanut peptides. The results indicate that FPHPP, FPHY, and FPHFD peptides have good thermal, pH, and digestive stability. MD trajectories elucidate the dynamic correlation between peptides and ACE and verify the specific binding interaction. Noteworthily, FPHPP is the best inhibitor with a strongest binding affinity and significantly increases NO, SOD production, and AT2R expression, and decreases ROS, MDA, ET-1 levels, ACE, and AT1R accumulation in Ang II-injury HUVEC cells.
具有低分子量、高生物利用度和良好吸收性的食物衍生肽已被开发为血管紧张素转换酶（ACE）抑制剂。在本研究中，进行了花生肽的体外抑制动力学、计算机筛选、ACE 抑制活性验证、分子动力学（MD）模拟和 HUVEC 细胞实验，以系统地鉴定 ACE 与花生肽相互作用的抑制机制。结果表明，FPHPP、FPHY 和 FPHFD 肽具有良好的热稳定性、pH 稳定性和消化稳定性。MD 轨迹阐明了肽与 ACE 之间的动态相关性，并验证了特定的结合相互作用。值得注意的是，FPHPP 是最好的抑制剂，具有最强的结合亲和力，并显著增加了 Ang II 损伤的 HUVEC 细胞中 NO、SOD 的产生和 AT2R 的表达，降低了 ROS、MDA、ET-1 水平、ACE 和 AT1R 的积累。
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