Virtual Screening of ACE Inhibitory Tripeptides Containing Tyrosine Residues Based on Molecular Docking

In order to obtain ACE inhibitory tripeptides containing tyrosine residues, the online Novopro database was used to construct tripeptides with tyrosine at the C-terminus for virtual screening to obtain tripeptides with selective inhibition of ACE-C domains, and predict their biological activity, water solubility, gastrointestinal absorbability, metabolism, and toxicity and other properties. The four ACE inhibitor peptides with high affinity to angiotensin-converting enzyme (ACE) were calculated by molecular docking, and the in vitro ACE inhibitory activity was determined to explore the relationship between binding sites and effects. The results showed that the four selected tripeptides RWY, FRY, YRY, and RFY had significant ACE inhibitory activity, with IC₅₀ values of 228.67, 113.10, 272.61, and 101.00 μmol/L, respectively. The virtual results of molecular docking showed that RWY, FRY, YRY, and RFY all had high affinity with S₁' pocket and produce hydrogen bond interactions. Among them, RFY combined with S₁' pocket to produce two hydrogen bonds had the best inhibitory effect. This article used bioinformatics principles to screen tyrosine tripeptides selectively inhibited by the ACE-C domain, providing new possibilities for high-speed screening of ACE inhibitor peptides.