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Novel Umami Peptide IPIPATKT with Dual Dipeptidyl Peptidase-IV and Angiotensin I-Converting Enzyme Inhibitory Activities

Mengdi Chen, Daodong Pan, Tianqiong Zhou, Xinchang Gao, Yali Dang

2021Journal of Agricultural and Food Chemistry67 citationsDOI

Abstract

A novel umami peptide, IPIPATKT, showed excellent dual dipeptidyl peptidase-IV (DPP-IV) and angiotensin I-converting enzyme (ACE) inhibitory activities, the IC50 values were 64 and 265 μM, respectively. Molecular docking displayed that IPIPATKT was docked into the S1 and S2 pockets of ACE, and it was close to the active site pocket of DPP-IV. The insulin-resistant-HepG2 (IR-HepG2) cell model and human umbilical vein endothelial cell (HUVEC) model showed that the peptide significantly increased the content of glucose, the activities of hexokinase, pyruvate kinase, and the concentration of nitric oxide (p < 0.01), while it reduced the content of endothelin-1 (ET-1). IPIPATKT exhibited a hypotensive effect (−23.5 ± 2.2 mmHg) and attenuated the increase in glucose levels in vivo, as demonstrated using spontaneous hypertensive rats (SHRs) and C57BL/6N mice. We reported the in vivo activities of the umami peptide with dual hypertensive and hypoglycemic effects for the first time.

Topics & Concepts

ChemistryDipeptidyl peptidaseDipeptidyl peptidase-4Nitric oxideIn vivoAngiotensin-converting enzymePeptideBradykininPharmacologyBiochemistryAngiotensin IIEnzymeEndocrinologyInternal medicineBiologyMedicineDiabetes mellitusType 2 diabetesReceptorBlood pressureBiotechnologyOrganic chemistryProtein Hydrolysis and Bioactive PeptidesBiochemical effects in animalsNeuropeptides and Animal Physiology
Novel Umami Peptide IPIPATKT with Dual Dipeptidyl Peptidase-IV and Angiotensin I-Converting Enzyme Inhibitory Activities | Litcius