Screening and mechanisms of novel angiotensin-I-converting enzyme inhibitory peptides from rabbit meat proteins: A combined in silico and in vitro study

Bioactive peptides derived from food proteins have various physiological roles and have attracted increasing attention in recent years. In this study, two novel ACE inhibitory peptides (EACF and CDF), screened from rabbit meat proteins using in silico methods, exhibited strong inhibitory effects in vitro. EACF and CDF were competitive and non-competitive inhibitors with half-maximal inhibitory concentrations of 41.06 ± 0.82 µM and 192.17 ± 2.46 µM, respectively. Molecular docking experiments revealed that EACF established eight H-bond interactions in the S1 and S2 pockets, and a metal-acceptor interaction with Zn 701. CDF shared four H-bond interactions in the S1 pocket of ACE. The results suggested that rabbit meat proteins could be a suitable material for the preparation of ACE inhibitory peptides, and that virtual screening is an effective, accurate and promising method for the discovery of novel active peptides.