Abstract: In our present study, virtual enzymatic hydrolysis of α-lactalbumin was investigated using online bioinformatic tools. The activity, toxicity, and physicochemical properties of the resulting bioactive peptides were predicted. A novel angiotensin I-converting enzyme (ACE) inhibitory peptide, Pro-Glu-Trp (PEW), was selected by molecular docking. PEW was synthesized by the solid phase method and its activity was verified in vitro, showing a half-maximal inhibitory concentration (IC50) value of 3 130 μmol/L. The molecular docking simulation results showed that the interaction between PEW and ACE’s active-site pocket S1 may be the major reason for its ACE inhibitory activity. Hydrogen bonding, hydrophobic force, and electrostatic force were the major forces maintaining their mutual binding. Compared with traditional methods, the protocol presented in this study could quickly and efficiently screen ACE inhibitory peptides, which may provide a new idea for the rapid screening of food-derived bioactive peptides.

Key words: virtual screening; molecular docking; angiotensin I-converting enzyme inhibitory peptide; α-lactalbumin