In this study, angiotensin-converting enzyme inhibitory peptides (ACE-IPs) derived from Muscovy duck (Cairina moschata) plasma hydrolysate (MDPH) were investigated. According to the general research protocol for bioactive peptides, the crude ACE-IPs of Muscovy duck plasma were separated and purified by ultrafiltration, gel chromatography and reversed-phase high-performance liquid chromatography (RP-HPLC). Then the components with the highest ACE inhibition potential were selected for identification. Finally, the inhibition mechanism was explored by molecular docking and in silico simulated digestion. A total of 121 peptides was detected, and five were screened for synthesis verification and molecular docking. The peptide VALSSLRP revealed high ACE inhibitory activity (91.67 ± 0.73%) because this peptide bound tightly to the S1' pocket and formed 3 hydrogen bonds. Meaningfully, this work provides some new information about the generation of ACE-IPs derived from duck blood plasma.
Keywords: ACE inhibitory peptide; Muscovy duck plasma; identification; molecule docking; purification.