From garlic proteins to bioactive peptides: A computer-aided screening for saltiness-enhancers and angiotensin I-converting enzyme inhibitors with mechanistic and kinetic analysis.

This study aimed to explore the potential of garlic proteins for producing multifunctional salty peptides. Three novel salty peptides (SNDPGR, SASDPNF, and ASTCMAR) were identified through simulated hydrolysis and in silico screening. Sensory evaluation and electronic tongue analysis confirmed their potent saltiness, with dose-dependent salt-enhancing effects further validated by the electronic tongue. Among them, SNDPGR exhibited the strongest activity. These peptides predominantly adopted random coil conformations, with varying proportions of α-helices and β-sheets. Molecular docking and dynamics simulations demonstrated that the salty peptides stably bound to the transmembrane channel-like 4 receptor mainly via hydrogen bonds. Moreover, all three salty peptides could inhibit ACE through forming extensive hydrogen bonding, electrostatic, and hydrophobic interactions with key active residues, with ASTCMAR showing the highest inhibition (IC50: 408.63 μmol/L). Such dual effects of salt reduction and ACE inhibition greatly enhanced the potential of these salty peptides as multifunctional food additives, offering promising strategies for the sustainable valorization of garlic proteins.