A novel angiotensin-I-converting enzyme inhibitory peptide from oyster: Simulated gastro-intestinal digestion, molecular docking, inhibition kinetics and antihypertensive effects in rats

Chen, Hui; Chen, Yu; Zheng, Huizhen; Xiang, Xingwei; Le, Xu

doi:10.3389/fnut.2022.981163

Cited by 6 publications

(4 citation statements)

References 57 publications

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“…The S1 pocket is composed of residues Ala354, Glu384 and Tyr523, whereas the S2 pocket includes Gln281, His353, Lys511, His513, and Tyr520. The primary catalytic center of the S3 pocket is the residue Glu162, which forms a tetrahedral structure through interactions with His383, His387, and Glu411 (Chen et al., 2022). As illustrated in Figure 7A, GPLGAL occupied the S1 pocket completely, establishing hydrogen bonds with Gln281 and His353 in the S2 pocket.…”

Section: Resultsmentioning

confidence: 99%

Two novel angiotensin‐converting enzyme (ACE) and dipeptidyl peptidase IV (DPP‐IV) inhibiting peptides from tilapia (Oreochromis mossambicus) skin and their molecular docking mechanism

Chen,

Ji,

Luo

et al. 2024

Journal of Food Science

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In the study, papain was used to hydrolyze tilapia (Oreochromis mossambicus) skin to obtain a tilapia skin hydrolysate (TSH) with dual angiotensin‐converting enzyme (ACE) and dipeptidyl peptidase IV (DPP‐IV) inhibitory activities. The resulting TSH was sequentially fractionated by ultrafiltration, size exclusion separation chromatography, and reverse‐phase high‐performance liquid chromatography. Its inhibitory effects on ACE and DPP‐IV were determined by commercial reagent kits. Two peptides purified from TSH were identified as Gly‐Pro‐Leu‐Gly‐Ala‐Leu (GPLGAL) and Lys‐Pro‐Ala‐Gly‐Asn (KPAGN) by the ultra‐performance liquid chromatography–tandem mass spectrometry (UPLC–MS/MS). Inhibitory concentration (IC50) of GPLGAL on ACE and DPP‐IV were 117.20 ± 1.69 and 187.10 ± 2.75 µM, respectively. IC50 of KPAGN on ACE and DPP‐IV were 137.40 ± 2.33 and 259.20 ± 2.85 µM, respectively. The molecular simulation demonstrated that the binding affinities of GPLGAL to ACE and DPP‐IV proteins were −8.5 and −7.4 kcal/mol, respectively, whereas those of KPAGN to ACE and DPP‐IV proteins were −7.9 and −6.7 kcal/mol, respectively. GPLGAL interacted with 21 amino acid residues of the ACE active site, whereas KPAGN engaged with 19 amino acid residues. Additionally, GPLGAL interacted with 10 amino acid residues of the DPP‐IV active site, whereas KPAGN engaged with 13 amino acid residues. The two peptides predominantly occupied the active sites of ACE (His513, Tyr523, and Ala354) and DPP‐IV (Tyr662 and Arg125) through hydrogen bonding. This leads to the deactivation of ACE and DPP‐IV.Practical ApplicationAccelerate tilapia skin development and high‐value utilization; provide foundation for preparing the peptides with dual ACE and DPP‐IV inhibiting activity.

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Section: Resultsmentioning

confidence: 99%

Two novel angiotensin‐converting enzyme (ACE) and dipeptidyl peptidase IV (DPP‐IV) inhibiting peptides from tilapia (Oreochromis mossambicus) skin and their molecular docking mechanism

Chen,

Ji,

Luo

et al. 2024

Journal of Food Science

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“…In vivo, the peptide effectively reduced SBP and DBP ( p < 0.01 in both) in hypertensive rats at 4 weeks. [ 44 ] So, it could be said that pearl oyster meat protein is a potential resource of ACE inhibitory peptides and their purified peptides could be exploited as functional food ingredients against HT.…”

Section: Resultsmentioning

confidence: 99%

Potential Impact of Bioactive Peptides from Foods in the Treatment of Hypertension

Ichim,

Marín,

Orenes‐Piñero

2024

Molecular Nutrition Food Res

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ScopeHigh blood pressure (BP) is the main preventable risk factor for cardiovascular diseases (CVDs). Much research is aimed at finding natural alternatives to control or prevent hypertension (HT), since some hypertensive patients do not respond to current pharmacological treatments or show undesirable side effects.Methods and resultsForty relevant articles have been selected from various scientific literature databases. The results reveal that angiotensin‐converting enzyme (ACE) inhibition is the most reported mechanism of action of antihypertensive peptides. The active peptides have a great variety of origins. Biopeptides with a molecular weight of <3 kDa, short chain <20 amino acids, and a hydrophobic amino acid sequence at the C‐ and N‐terminus exhibit higher antihypertensive activity. They also show good stability to enzymatic hydrolysis and gastrointestinal digestion, and no toxicity. To determine antihypertensive effectiveness, in vitro and in vivo animal studies are the most frequent developed, with few in silico studies and only one human clinical trial.ConclusionThere is interesting potential for antihypertensive peptides as promising natural candidates for the development of functional foods, nutraceuticals and drugs for preventive or therapeutic treatment of hypertension. The aim of this review is to study the role of food‐derived bioactive peptides in HT.

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“…Wu et al [49] reported that peptides with higher hydrophobicity exhibit a greater inhibitory activity. Other studies [39,[50][51][52] have also shown that peptides containing leucine have significant ACE inhibitory potential. Olalere et al [53] analysed the profile of all peptides described as ACE inhibitors in the BIOPEP-UWM virtual database [54], and found that the presence of branched aliphatic amino acids, such as leucine, in the C1 position was highly noticeable in ACE inhibitory peptides.…”

Section: Identification Of the Peptide Composition Of The Most Potent...mentioning

confidence: 91%

Protein Hydrolysis as a Way to Valorise Squid-Processing Byproducts: Obtaining and Identification of ACE, DPP-IV and PEP Inhibitory Peptides

Bougatef,

Sila,

Bougatef

et al. 2024

Marine Drugs

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The industrial processing of Argentine shortfin squid to obtain rings generates a significant amount of protein-rich waste, including the skin, which is rich in collagen and attached myofibrillar proteins. This waste is generally discarded. In this study, skin was used as a source of proteins that were hydrolysed using Trypsin, Esperase® or Alcalase®, which released peptides with antioxidant potential and, in particular, antihypertensive (ACE inhibition), hypoglycemic (DPP-IV inhibition) and/or nootropic (PEP inhibition) potential. Among the three enzymes tested, Esperase® and Alcalase produced hydrolysates with potent ACE-, DPP-IV- and PEP-inhibiting properties. These hydrolysates underwent chromatography fractionation, and the composition of the most bioactive fractions was analysed using HPLC-MS-MS. The fractions with the highest bioactivity exhibited very low IC50 values (16 and 66 µg/mL for ACE inhibition, 97 µg/mL for DPP-IV inhibition and 55 µg/mL for PEP inhibition) and were mainly derived from the hydrolysate obtained using Esperase®. The presence of Leu at the C-terminal appeared to be crucial for the ACE inhibitory activity of these fractions. The DPP-IV inhibitory activity of peptides seemed to be determined by the presence of Pro or Ala in the second position from the N-terminus, and Gly and/or Pro in the last C-terminal positions. Similarly, the presence of Pro in the peptides present in the best PEP inhibitory fraction seemed to be important in the inhibitory effect. These results demonstrate that the skin of the Argentine shortfin squid is a valuable source of bioactive peptides, suitable for incorporation into human nutrition as nutraceuticals and food supplements.

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A novel angiotensin-I-converting enzyme inhibitory peptide from oyster: Simulated gastro-intestinal digestion, molecular docking, inhibition kinetics and antihypertensive effects in rats

Cited by 6 publications

References 57 publications

Two novel angiotensin‐converting enzyme (ACE) and dipeptidyl peptidase IV (DPP‐IV) inhibiting peptides from tilapia (Oreochromis mossambicus) skin and their molecular docking mechanism

Two novel angiotensin‐converting enzyme (ACE) and dipeptidyl peptidase IV (DPP‐IV) inhibiting peptides from tilapia (Oreochromis mossambicus) skin and their molecular docking mechanism

Potential Impact of Bioactive Peptides from Foods in the Treatment of Hypertension

Protein Hydrolysis as a Way to Valorise Squid-Processing Byproducts: Obtaining and Identification of ACE, DPP-IV and PEP Inhibitory Peptides

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