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

• Published in: Journal of functional foods 2022-01, Vol.88, p.104892, Article 104892
• Main Authors: Urbizo-Reyes, Uriel, Liceaga, Andrea M., Reddivari, Lavanya, Kim, Kee-Hong, Anderson, Joseph M.
• Format: Article
• Language: English
• Subjects: Angiotensin converting enzyme; Biopeptides; Canary seed; Molecular docking; Pancreatic lipase
• ISSN: 1756-4646; 2214-9414
• DOI: 10.1016/j.jff.2021.104892

[Display omitted] •Canaryseed peptides (CSP) exhibit ACE and pancreatic lipase inhibition activity.•CSP retained bioactiviy after gastrointestinal digestion (CSP-SGD)•CSP-SGD peptides interfered with the lid domain function of pancreatic lipase.•Zn(II) coordination and destabilization of the transition state reduced ACE activity.•CSP-SGD displayed good bioavailablility (>10%) in a Caco-2 model. 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 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 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.