Enzyme kinetics, molecular docking, and in silico characterization of canary seed (Phalaris canariensis L.) peptides with ACE and pancreatic lipase inhibitory activity

The bioactivity of canary seed peptides (CSP) towards metabolism-regulating enzymes was evaluated. Peptides with angiotensin-converting enzyme (ACE), dipeptidyl peptidase IV (DPP-IV), and pancreatic lipase activity remained stable (p < 0.05) to simulated gastrointestinal digestion (SGD). CSP-SGD were transported efficiently (>10%) through the Caco-2 monolayer, indicating absorption intestinal epithelium. Lineweaver-Burk plots demonstrated that act as mixed-type inhibitors for DPP-IV α-glucosidase. Furthermore, potent antihypertensive antiobesity agents. Molecular docking in silico analyses targeted understand interactions ACE lipase. ACE-inhibitory (LHPQ, QTPHQ, KPVPR, ELHPQ) acted non-competitive by destabilization transition state Zn(II) coordination ACE. uncompetitive inhibition (VPPR, LADR, LSPR, TVGPR) destabilized open-lid conformation results this study showed proteins could serve a source biologically active peptides.