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Enzyme Kinetics, Molecular Docking, And In Silico Characterization Of Canary Seed (Phalaris Canariensis L.) Peptides With Ace And Pancreatic Lipase Inhibitory Activity, Uriel Urbizo-Reyes, Andrea M. Liceaga, Lavanya Reddivari, Kee-Hong Kim, Joseph M. Anderson
Enzyme Kinetics, Molecular Docking, And In Silico Characterization Of Canary Seed (Phalaris Canariensis L.) Peptides With Ace And Pancreatic Lipase Inhibitory Activity, Uriel Urbizo-Reyes, Andrea M. Liceaga, Lavanya Reddivari, Kee-Hong Kim, Joseph M. Anderson
Department of Food Science Faculty Publications
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 through the intestinal epithelium. Lineweaver-Burk plots demonstrated that CSP-SGD act as mixed-type inhibitors for DPP-IV and α-glucosidase. Furthermore, CSP-SGD were potent as antihypertensive and antiobesity agents. Molecular docking and in silico analyses were targeted to understand CSP-SGD interactions with ACE and pancreatic lipase. ACE-inhibitory peptides (LHPQ, QTPHQ, KPVPR, and ELHPQ) acted as non-competitive inhibitors by destabilization of the transition state and Zn(II) coordination in …