Investigation on the characteristics and mechanisms of ACE inhibitory peptides by a thorough analysis of all 8000 tripeptides via binding free energy calculation

Food-derived angiotensin I-converting enzyme (ACE) inhibitory peptides represent a potential source of new antihypertensive. However, their characteristics and binding mechanisms were not well understood. In this study, novel energy calculation experimentation combined to elucidate the ACE tripeptides. activity all 8,000 tripeptides was investigated by in silico experiments. IC50 values five top-rated ranged from 5.86 21.84 ?M. Five hundred top-ranked chosen for detailed structure–activity analysis, significant preference aromatic amino acids at both C- N-terminus found. By free analysis nine representative via MM/GBSA, electrostatic found be leading that contributed with its high affinity Besides, S355, V380, V518, three residues positioned around classical pockets ACE, also played key role ACE's binding. Therefore, tripeptides, redefined. conclusion, more deeply illustrated thorough The allows better understanding peptides, which could used redesign inhibitors stronger activity.