AI Article Synopsis
- Food-derived peptides, particularly from peanuts, have been studied as effective inhibitors of angiotensin-converting enzyme (ACE), which plays a role in hypertension and cardiovascular health.
- The research involved both in vitro tests and computational methods to confirm the peptides' inhibitory effects and understand their mechanisms of action.
- Among the tested peptides, FPHPP was identified as the most potent, demonstrating strong binding affinity and beneficial effects on cell health markers related to oxidative stress and inflammation.
Article Abstract
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.
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| http://dx.doi.org/10.1016/j.ijbiomac.2024.131901 | DOI Listing |
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