In-silico identification and molecular docking analysis of ACE-inhibitory peptides derived from soybean glycinin

This study explored the potential of soybean glycinin as a source of natural ACE-inhibitory peptides, given the limitations and side effects associated with conventional synthetic ACE inhibitors. Following in silico enzymatic hydrolysis by chymotrypsin and pepsin, the released peptides were identified and their potential ACE-inhibitory activity was assessed. Molecular docking analysis revealed that two peptides, PSY and VVF, exhibited the strongest binding affinity toward ACE (- 7 Kcal/mol). Among them, PSY formed a broader and more stable interaction network within the active site of ACE, suggesting a higher inhibitory potential compared to other peptides. Overall, the findings indicate that soybean glycinin is a promising source of natural ACE inhibitors and can be further explored for the development of antihypertensive functional foods and supplements.