Enzyme kinetics, molecular docking, and in silico characterization of canary seed (Phalaris canariensis L.) peptides with ACE and pancreatic lipase inhibitory activity. (January 2022)

• Record Type: Journal Article
• Authors: Urbizo-Reyes, Uriel; Liceaga, Andrea M.; Reddivari, Lavanya; Kim, Kee-Hong; Anderson, Joseph M.
• Is Part Of: Journal of functional foods. Volume 88(2022)
• Publication Date: 2022-01
• Subjects: Canary seed -- Biopeptides -- Molecular docking -- Pancreatic lipase -- Angiotensin converting enzyme; Functional foods -- Analysis -- Periodicals; Food -- Biotechnology -- Periodicals; Nutrition -- Periodicals; 613.2
• DOI: 10.1016/j.jff.2021.104892
• Languages: English
• ISSNs: 1756-4646

Abstract

Graphical abstract: Highlights: 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. Abstract: 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 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.