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

Autor: Uriel Urbizo-Reyes, Andrea M. Liceaga, Lavanya Reddivari, Kee-Hong Kim, Joseph M. Anderson
Jazyk: angličtina
Rok vydání: 2022
Předmět:
Zdroj: Journal of Functional Foods, Vol 88, Iss , Pp 104892- (2022)
Druh dokumentu: article
ISSN: 1756-4646
DOI: 10.1016/j.jff.2021.104892
Popis: 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.
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