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

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.

Exploration of Dipeptidyl Peptidase-IV (DPP-IV) Inhibitory Peptides from Silkworm Pupae (Bombyx mori) Proteins Based on In Silico and In Vitro Assessments

“…Ala-Asp-Phe, Met-Ile-Arg, and Phe-Gly-Arg were identified and screened from egg protein with the IC 50 values of 16830, 4860, and 46220 μM, respectively . The measured IC 50 value of Ile-Pro-Ile-Pro-Ala-Thr-Lys-Asn identified from Sanhuang chicken protein was 265 μM . In this work, the determined IC 50 values of Leu-Pro-Pro-Glu-His-Asp-Trp-Arg and Leu-Pro-Ala-Val-Thr-Ile-Arg derived from silkworm pupae proteins were close to the IC 50 values of several previously reported DPP-IV inhibitory peptides, Ala-Pro (259.62 μM) and Ile-Pro-Ala (110.37 μM) identified from Antarctic krill peptides .…”

Research progress in the screening and evaluation of umami peptides

“…In addition, peptides extracted from animal and plant proteins also have an umami taste, which are called umami peptides (Zhang et al., 2017). Because of their palatability, complicated taste, and multiple biological functions (Chen, Pan, et al., 2021; Hao et al., 2020; Shen et al., 2021; Zhang, Pan, et al., 2021), the discovery and identification of new umami peptides from foodborne proteins have attracted increasing attention (Li et al., 2020). The classical method of using column chromatography to separate and purify umami peptides, however, is usually time‐consuming and expensive (Sun et al., 2017), which has limited the development of industrialization of umami peptides.…”

Preparation, Characterization, and Cytoprotective Effects on HUVECs of Fourteen Novel Angiotensin-I-Converting Enzyme Inhibitory Peptides From Protein Hydrolysate of Tuna Processing By-Products

“…As a known vasoconstriction factor, ET-1 is similar to Ang II and can lead to endothelial dysfunction related to hypertension and atherosclerosis. Previous reports confirmed that GRVSNCAA and TYLPVH from R. philippinarum gave play to their hypotensive activity by prominently reducing ET-1 generation ( 64 ), and the umami octapeptide of IPIPATKT could decrease the content of endothelin-1 (ET-1) in insulin-resistant-HepG2 cell and HUVECs models ( 71 ). In addition, ADVFNPR, VVLWK, LPILR, and VIEPR presented potent noncompetitive ACEi activity and significantly decreased the ET-1 levels in EA.hy926 cells ( 72 ).…”