Studies on the Interaction between Angiotensin-Converting Enzyme (ACE) and ACE Inhibitory Peptide from <i>Saurida elongata</i>

Lan, Xin; Sun, Lixia; Muhammad, Yaseen; Wang, Zefen; Liu, Haibo; Sun, Jianhua; Zhou, Liqin; Feng, Xuezhen; Liao, Dankui; Wang, Shuangfei

doi:10.1021/acs.jafc.8b04303

Cited by 38 publications

(23 citation statements)

References 43 publications

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“…The molecular docking study revealed that NIFRPF formed hydrogen bonds with the S1 pocket (Ala 354, Glu 384 and Tyr 523) and established direct interaction with Zn (II), which could explain its inhibition effect against ACE activity. However, previous research showed that some ACE inhibitory peptides, such as QAGLSPVR and GMKCAF, based on a non‐competitive inhibition mechanism, could not interact with the active site of ACE 39, 40 . Therefore, it might be reasonable that peptides FHPFPR and NWFPLPR did not interact with main active sites of ACE in the current study.…”

Section: Resultsmentioning

confidence: 69%

“…However, previous research showed that some ACE inhibitory peptides, such as QAGLSPVR and GMKCAF, based on a non-competitive inhibition mechanism, could not interact with the active site of ACE. 39,40 Therefore, it might be reasonable that peptides FHPFPR and NWFPLPR did not interact with main active sites of ACE in the current study.…”

Section: Novel Ace Inhibitory Peptides and Molecular Dockingmentioning

confidence: 76%

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Antihypertensive effect of quinoa protein under simulated gastrointestinal digestion and peptide characterization

et al. 2020

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BACKGROUND: Quinoa protein is a potential source of bioactive peptides. Although some studies have demonstrated its angiotensin converting enzyme (ACE) inhibitory properties, research into its in vivo effect on blood-pressure regulation and peptide characterization remains limited. RESULTS: Quinoa protein hydrolyzate (QPH) was prepared by simulated gastrointestinal digestion. QPH lowered the systolic blood pressure (SBP) and diastolic blood pressure (DBP) in spontaneously hypertensive model rats (SHRs) from 2 h to10 h after oral administration, effectively controlling blood pressure in these SHRs. An in vitro study showed that QPH is capable of inhibiting ACE activity. This was attributed to the activity of a number of low-molecular-weight peptides. With relatively high scores predicted by PeptideRanker, three promising bioactive peptides, FHPFPR, NWFPLPR, and NIFRPF, were further studied and their ACE-inhibition effects were confirmed with IC 50 values of 34.92, 16.77, and 32.40 ∼M, respectively. A molecular docking study provided insights into the binding of ACE with peptides, and revealed that the presence of specific amino acids in the peptide sequence (Pro, Phe, and Arg at the C-terminal, and Asn at the N-terminal) could contribute to the interaction between ACE and peptides. CONCLUSION: These results demonstrated the potential of QPH for the management of hypertension, which indicates that it could be a good candidate for inclusion in functional foods to control high blood pressure.

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Section: Resultsmentioning

confidence: 69%

Section: Novel Ace Inhibitory Peptides and Molecular Dockingmentioning

confidence: 76%

Antihypertensive effect of quinoa protein under simulated gastrointestinal digestion and peptide characterization

et al. 2020

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“…Compared with microorganism fermentation and chemical degradation processes, proteolytic hydrolysis method has been widely used because of its advantages of easy control, environmental friendliness, no residual chemical reagents, or no harmful substances (20,57,58). The biological activities of protein hydrolysates are closely contacted with the biopeptide composition, and specificity of enzymes is the key factor affecting those properties (59,60).…”

Section: Preparation Of Milt Protein Hydrolysatementioning

confidence: 99%

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

et al. 2022

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To prepare peptides with high angiotensin-converting enzyme (ACE) inhibitory (ACEi) activity, Alcalase was screened from five proteases and employed to prepare protein hydrolysate (TMH) of skipjack tuna (Katsuwonus pelamis) milts. Subsequently, 10 novel ACEi peptides were isolated from the high-ACEi activity TMH and identified as Tyr-Asp-Asp (YDD), Thr-Arg-Glu (TRE), Arg-Asp-Tyr (RDY), Thr-Glu-Arg-Met (TERM), Asp-Arg-Arg-Tyr-Gly (DRRYG), Ile-Cys-Tyr (ICY), Leu-Ser-Phe-Arg (LSFR), Gly-Val-Arg-Phe (GVRF), Lys-Leu-Tyr-Ala-Leu-Phe (KLYALF), and Ile-Tyr-Ser-Pro (IYSP) with molecular weights of 411.35, 404.41, 452.45, 535.60, 665.69, 397.48, 521.61, 477.55, 753.91, and 478.53 Da, respectively. Among them, the IC50 values of ICY, LSFR, and IYSP on ACE were 0.48, 0.59, and 0.76 mg/mL, respectively. The significant ACEi activity of ICY, LSFR, and IYSP with affinities of −7.0, −8.5, and −8.3 kcal/mol mainly attributed to effectively combining with the ACEi active sites through hydrogen bonding, electrostatic force, and hydrophobic interaction. Moreover, ICY, LSFR, and IYSP could positively influence the production of nitric oxide (NO) and endothelin-1 (ET-1) secretion in human umbilical vein endothelial cells (HUVECs) and weaken the adverse impact of norepinephrine (NE) on the production of NO and ET-1. In addition, ICY, LSFR, and IYSP could provide significant protection to HUVECs against H2O2 damage by increasing antioxidase levels to decrease the contents of reactive oxide species and malondialdehyde. Therefore, the ACEi peptides of ICY, LSFR, and IYSP are beneficial functional molecules for healthy foods against hypertension and cardiovascular diseases.

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“…Usually, the ACE inhibitory peptide functions by directly binding to ACE. The interaction between ACE and peptides was demonstrated in kinetic studies and molecular docking simulations. − …”

Section: Introductionmentioning

confidence: 99%

Novel ACE Inhibitory Peptides Derived from Yeast Hydrolysates: Screening, Inhibition Mechanisms and Effects on HUVECs

Huang

Feng

Zhao

et al. 2021

J. Agric. Food Chem.

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The antihypertensive activity of yeast hydrolysate (YH) was confirmed in our previous study. However, the critical peptides in YH and the underlying mechanisms have not been fully elucidated. This study aimed to explore the angiotensin-converting enzyme (ACE) inhibitory peptides in YH and illustrate their molecular and cellular mechanisms. The potential of YH-derived peptides was evaluated by in silico methods, followed by in vitro verification. A new competitive ACE inhibitory peptide, VIPVPFF (V7), with an IC50 value of 10.27 μM, was screened. YH and V7 increased the nitric oxide (NO) levels, upregulated GUCY1A1 gene expression (approximately 15-fold), and functioned in several hypertension-related pathways in human umbilical vein endothelial cells (HUVECs). This study revealed the antihypertensive mechanisms of YH and V7, laying down a theoretical basis for their application.

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Studies on the Interaction between Angiotensin-Converting Enzyme (ACE) and ACE Inhibitory Peptide from Saurida elongata

Cited by 38 publications

References 43 publications

Antihypertensive effect of quinoa protein under simulated gastrointestinal digestion and peptide characterization

Antihypertensive effect of quinoa protein under simulated gastrointestinal digestion and peptide characterization

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

Novel ACE Inhibitory Peptides Derived from Yeast Hydrolysates: Screening, Inhibition Mechanisms and Effects on HUVECs

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