ACE inhibitory activities of two peptides derived from Volutharpa ampullacea perryi hydrolysate and their protective effects on H2O2 induced HUVECs injury

Wang, Chenxin; Song, Chengcheng; Liu, Xintong; Qiao, Bian-Wen; Song, Shuang; Fu, Yinghuan

doi:10.1016/j.foodres.2022.111402

Cited by 13 publications

(17 citation statements)

References 44 publications

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“…In addition, PG-7 revealed to be more effective than KA-8 in improving Ang II-induced abnormalities in eNOS and ET-1 levels. These results are in concordance with the previous studies, where peptides IVTNWDDMEK, IPIPATKT, and LSGYGP confirmed the improvement effects in eNOS and ET-1 levels. ,, In summary, our research suggested that two peptides, especially PG-7, may improve endothelial cell dysfunction and decrease blood pressure by regulating the eNOS expression and ET-1 secretion.…”

Section: Discussionsupporting

confidence: 93%

“…The results showed that the binding force of ACE and peptides was not only related to the number and length of hydrogen bonds but also to other forces such as hydrophobic force and van der Waals force. This result was consistent with the previous research . Furthermore, the results of ACE inhibition of two peptides in vitro also showed that PG-7 had ACE inhibition activity stronger than KA-8.…”

Section: Discussionsupporting

confidence: 93%

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Peptides from Harpadon nehereus Bone Ameliorate Angiotensin II-Induced HUVEC Injury and Dysfunction through Activation of the AKT/eNOS and Nrf2 Pathway

Shao,

Zhao,

Shen

et al. 2023

ACS Omega

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Angiotensin II (Ang II)-induced vascular endothelial cell injury and dysfunction are important pathophysiological factors in the occurrence and development of hypertension. In this study, the amelioration effects of two peptides KA-8 (KLHDEEVA) and PG-7 (PSRILYG) from Harpadon nehereus bone on Ang II-induced damage and dysfunction in human umbilical vein endothelial cells (HUVECs) were investigated. The results showed that they could significantly decrease the reactive oxygen species (ROS) level and increase the activity of antioxidant enzymes in Ang II-induced HUVEC. Two peptides, especially PG-7, significantly upregulated the expression of nuclear factor erythroid 2-related factor 2 (Nrf2). In addition, PG-7 significantly reduced the level of expression of endothelin-1(ET-1) and increased the phosphorylation level of phosphoinositide 3-kinase (PI3K), serine/threonine kinase (AKT), and nitric oxide synthase (eNOS). These results indicated that the two peptides, especially PG-7, can ameliorate angiotensin II-induced HUVEC injury and dysfunction through activation of the AKT/eNOS and Nrf2 pathway. Furthermore, PG-7 showed a stronger affinity with angiotensin-converting enzyme (ACE) and ACE inhibitory than KA-8. In conclusion, peptide PG-7 reveals potential in the prevention and treatment of hypertension.

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Section: Discussionsupporting

confidence: 93%

Section: Discussionsupporting

confidence: 93%

Peptides from Harpadon nehereus Bone Ameliorate Angiotensin II-Induced HUVEC Injury and Dysfunction through Activation of the AKT/eNOS and Nrf2 Pathway

Shao,

Zhao,

Shen

et al. 2023

ACS Omega

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“…Previous studies have demonstrated the interactions between ACE and various peptides by analyzing molecular docking. , There are three pockets in the active site of ACE, including S1, S2, and S1′. The S1 pocket involves Ala354, Glu384, and Tyr523; the S2 pocket contains Gln281, His353, Lys511, His513, and Tyr520; and the S1′ pocket contains Glu162 …”

Section: Resultsmentioning

confidence: 99%

“…The sequence of the peptides is crucial for their function. , Peptides with 2–12 amino acids show more robust ACE inhibitory activity than high-molecular-weight peptides because low-molecular-weight peptides are more likely to bind to ACE active sites …”

Section: Discussionmentioning

confidence: 99%

“…ACE inhibitory peptides P3 (LIVGFPAYGH) and P12 (IVGFPAYGH) have both hydrophobic (Gly, Ala, Val, Phe, and Pro) and hydrophilic (His and Tyr) amino acids. Aliphatic amino acids (Leu and Ile) were frequently found in the N-terminus of ACE inhibitory peptides, such as peptides from soy protein (LIVTQ and LIVT) and Volutharpa ampullacea perryi (IVTNWDDMEK) . Positively charged amino acids (His) were reported to be a critical residue in the C-terminus tripeptide position of ACE inhibitory peptides, such as fermented milk (LVYPFPGPIH), Tenebrio molitor (YDDGSYKPH), horse gram flour (VTSTGPVGH), and porcine plasma proteins (YTFPFH) .…”

Section: Discussionmentioning

confidence: 99%

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Angiotensin I-Converting Enzyme Inhibitory Activity of Two Peptides Derived from In Vitro Digestion Products of Pork Sausage with Partial Substitution of NaCl by KCl

Zou

Zhou

et al. 2023

J. Agric. Food Chem.

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This study aimed to identify angiotensin I-converting enzyme (ACE) from in vitro digestion products of pork sausage with partial substitution of NaCl by KCl (PSRK). Peptides from in vitro digestion products of PSRK were identified through liquid chromatography with tandem mass spectrometry analysis coupled with de novo sequencing. Subsequently, the ACE inhibitory peptides LIVGFPAYGH and IVGFPAYGH were screened based on PeptideRanker, in silico absorption, molecular docking, and the determination of ACE inhibitory activity. In addition, the ACE inhibitory peptides LIVGFPAYGH and IVGFPAYGH were mixedtype inhibitors; these peptides' ACE inhibitory activities were expressed as the 50% inhibitory concentration (IC 50 ) values in vitro, which were 196.16 and 150.88 μM, respectively. After 2 h of incubation, LIVGFPAYGH and IVGFPAYGH could be transported through Caco-2 cell monolayers with paracellular passive diffusion. Furthermore, LIVGFPAYGH and IVGFPAYGH significantly increased the levels of ACE2 and nitric oxide while decreasing the levels of ACE, angiotensin II, and endothelin-1 in Ang I-treated human umbilical vein endothelial cells, indicating the ACE inhibitory effect of LIVGFPAYGH and IVGFPAYGH. In summary, LIVGFPAYGH and IVGFPAYGH from PSRK can be used as functional foods with antihypertensive activity.

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A novel alcalase-hydrolyzed soybean meal hydrolysates prepared using by-product material: Structure, function property, sensory property, and biological activity

Zhang,

Du,

et al. 2023

Food Bioscience

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ACE inhibitory activities of two peptides derived from Volutharpa ampullacea perryi hydrolysate and their protective effects on H2O2 induced HUVECs injury

Cited by 13 publications

References 44 publications

Peptides from Harpadon nehereus Bone Ameliorate Angiotensin II-Induced HUVEC Injury and Dysfunction through Activation of the AKT/eNOS and Nrf2 Pathway

Peptides from Harpadon nehereus Bone Ameliorate Angiotensin II-Induced HUVEC Injury and Dysfunction through Activation of the AKT/eNOS and Nrf2 Pathway

Angiotensin I-Converting Enzyme Inhibitory Activity of Two Peptides Derived from In Vitro Digestion Products of Pork Sausage with Partial Substitution of NaCl by KCl

A novel alcalase-hydrolyzed soybean meal hydrolysates prepared using by-product material: Structure, function property, sensory property, and biological activity

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