Purification and characterization of a novel angiotensin I‐converting enzyme‐inhibitory peptide derived from Alaska pollack skins

Abstract

Hydrolysates containing angiotensin I‐converting enzyme (ACE)‐inhibitory peptide were prepared from protein of Alaska pollack skins using alcalase and trypsin. The protein hydrolysate was separated by ultrafiltration, Sephadex G‐25 gel filtration chromatography and reversed phase high‐performance liquid chromatography (HPLC), from which a novel purified peptide was obtained. Both random coil structure and β‐sheet in the purified peptide were revealed in Fourier transform infrared spectrum. The amino sequence of the purified peptide was identified as GPLGVP, VLYPVK, VFLENVLR, and FEEF by HPLC‐Q‐TOF‐MS (HPLC‐quadrupole time‐of‐flight mass spectrometry). The peptide GPLGVP whose molecular weight was 538.31 Da showed the highest ACE inhibitory activity (IC50 = 105.8 µM). The purified peptide featured a noncompetitive inhibition kinetic mechanism was shown in the Lineweaver–Burk plots and was susceptible to enzymes as indicated in the studies on stability of gastrointestinal proteases. Moreover, the peptide GPLGVP can combine ACE catalytic pocket through hydrogen bonds and other forces with high binding power as disclosed in molecular docking simulation, which provides the inhibitory effect of GPLGVP on ACE.

Novel angiotensin-converting enzyme inhibitory peptides from tuna byproducts—milts: Preparation, characterization, molecular docking study, and antioxidant function on H2O2-damaged human umbilical vein endothelial cells

“…Those fish byproducts result in burdensome disposal problems, and unreasonable treatment will give rise to serious environmental pollution (24-26). For making full use of these fish byproducts, many ACEi peptides were prepared from different processing byproducts, such as tuna bone (27, 28), skate (Okamejei kenojei) skin (29), mackerel skin (30), Nile tilapia skin (31) and skeleton (32), sea cucumber (Stichopus japonicus) gonad (33), smooth-hound (Mustelus mustelus) viscera (34), Atlantic salmon skin (35), Alaska pollack skins (36), and rainbow trout (Oncorhynchus mykiss) viscera (37). Those sea-food derived ACEi peptides exhibit high potential application value in terms of diet and clinical therapeutics on anti-hypertension (5,38,39).…”

Formation and inhibition mechanism of novel angiotensin I converting enzyme inhibitory peptides from Chouguiyu

“…There were 14 kinds of interactions found in complexes of seven ACE inhibitory peptides and ACE, belonging to electrostatic interaction (attractive charge, pi-anion, and pi-cation), hydrogen bond (salt bridge, conventional hydrogen bond, carbon-hydrogen bond, and pi-donor hydrogen bond), hydrophobic interaction (pi-pi T-shaped, pi-sigma, alkyl, and pi-alkyl), and other interaction (pi-sulfur and sulfur-X). Hydrogen bond and hydrophobic interaction are considered the main interactions between ACE inhibitory peptides and ACE (4,8). In this study, plenty of salt bridges, conventional hydrogen, carbon-hydrogen bond, and alkyl were found between the 7 ACE inhibitory peptides and ACE.…”

“…Molecular docking technology has been widely used to study the ACE inhibition mechanism of peptides (4,8). In this study, the energy of molecular docking between ACE and ACE inhibitory peptides is shown in Supplementary Table S4.…”

“…Many drugs have been designed to inhibit ACE, such as captopril and lisinopril, but synthetic drugs have many side effects (3). A large number of food-derived peptides have been identified as potential substitutes for synthetic drugs to treat hypertension (4,5). These inhibitory peptides have distinct structural characteristics, such as possessing fewer amino acids, abundant hydrophobic amino acids, and aliphatic, aromatic, or positively charged amino acids in the N/C terminal (6,7).…”

Isolation, identification, molecular docking analysis, and cytoprotection of seven novel angiotensin I-converting enzyme inhibitory peptides from miiuy croaker byproducts-swim bladders

“…Those fish byproducts will lead to serious environmental problems if they can't be handled properly (Zhang et al, 2019;Yang et al, 2019a). To make full use of these fish byproducts, many ACEi peptides were prepared from different processing byproducts, such as tuna black muscle and bone (Lee et al, 2010;Qiao et al, 2022), smooth-hound viscera (Abdelhedi et al, 2017;Abdelhedi et al, 2018), cuttlefish muscle (Balti et al, 2015), Nile tilapia skeleton (Borges-Contreras et al, 2019), rainbow trout viscera (Vaśquez et al, 2022) [34], and Alaska pollack skins (Yang et al, 2021). Those sea-food derived ACEi peptides exhibit high potential application value in diet or clinical treatment on antihypertension (Abdelhedi and Nasri, 2019;Fan et al, 2019).…”