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 through the intestinal epithelium. LineweaverBurk plots demonstrated that CSP-SGD act as mixed-type inhibitors for DPP-IV and alpha-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 ACE. The uncompetitive inhibition of pancreatic lipase by peptides (VPPR, LADR, LSPR, and TVGPR) destabilized the open-lid conformation of pancreatic lipase. The results of this study showed that canary seed proteins could serve as a source of biologically active peptides.

Automated summary

This study evaluated the bioactivity of canary seed peptides towards metabolism-regulating enzymes and found that they have antihypertensive and antiobesity effects. Molecular docking and in silico analyses revealed the interaction mechanisms between canary seed proteins and ACE and pancreatic lipase.