A novel Angiotensin-I-converting enzyme (ACE) inhibitory peptide IAF (Ile-Ala-Phe) from pumpkin seed proteins: in silico screening, inhibitory activity, and molecular mechanisms

Liang, Fuqiang; Shi, Yumeng; Shi, Jiayi; Zhang, Tai; Zhang, Ran

doi:10.1007/s00217-021-03783-1

Cited by 24 publications

(11 citation statements)

References 37 publications

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“…Liang et al [ 11 ] identified a peptide IAF from pumpkin seeds using in silico approaches. By molecular docking, a strong interaction was found between IAF and ACE, which shows hydrogen bonding between two residues of ACE, His513 and Glu162, with IAF.…”

Section: Introductionmentioning

confidence: 99%

[Retracted] Exploration of ACE‐Inhibiting Peptides Encrypted in Artemisia annua Using In Silico Approach

Shahid

Zawar

Jamal

et al. 2022

BioMed Research International

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The renin-angiotensin system (RAS) is involved in body fluid regulation, but one of its enzymes, angiotensin-converting enzyme (ACE), indirectly causes hypertension by constricting blood vessels. Autoimmune illness is linked to the increased risk of hypertension and cardiovascular disease. In this study, ACE-inhibiting peptides were studied from Artemisia annua proteins. In silico hydrolysis of proteins was performed by BIOPEP-UWM using proteolytic enzymes from plant, microbial, and digestive sources. The physicochemical properties of 1160 peptides were determined using the peptide package of R studio. Di- and tripeptides were mostly released with a molecular weight of 170 to 350 Da. PeptideRanker was used to select 16 peptides from a pool of 1160 peptides based on their likelihood of being bioactive. Molecular docking was performed by DS 2020 and AutoDock Vina, which revealed that the stability of the ligand-receptor complex is due to hydrogen bonding and electrostatic and hydrophobic interactions. Their binding energies ranged from -31.81 to -20.09 kJ/mol. For drug-likeness evaluation, an online tool SwissADME was used that follows the ADME rule (absorption, distribution, metabolism, and excretion) to check the pharmacokinetics and drug-likeness of the compound. In the future, the released peptides can be used to make functional nutraceutical foods against hypertension.

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Section: Introductionmentioning

confidence: 99%

[Retracted] Exploration of ACE‐Inhibiting Peptides Encrypted in Artemisia annua Using In Silico Approach

Shahid

Zawar

Jamal

et al. 2022

BioMed Research International

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“…However, activating ACE2 activity is not a common feature of ACE inhibitory peptides as confirmed in the study by Wang et al, 48 which found 8 (IQP, YQY, MRW, RIY, IKP, FFY, AKK, and IEF) out of 20 selected ACE inhibitory peptides had no effects on ACE2 levels. Although peptides with ACE inhibition activity had been previously identified from pumpkin seed proteins, 17,19,20 SNHANQLDFHP and PVQVLASAYR obtained in this study were the first PSM-derived peptides reported to have both ACE inhibition and ACE2 upregulation activities in endothelial cells. In conclusion, the present results indicated that SNHANQLDFHP and PVQVLASAYR had the ability to increase the release of NO, decrease the secretion of ET-1, and regulate ACE2 activity in EA.hy926 cells, which had positive effects on the protection of EA.hy926 cells and the treatment of hypertension.…”

Section: ■ Discussionmentioning

confidence: 82%

“…The hydrolysates of PSM have a wide range of physiological activities , including antihypertensive activity. In the previous studies, Liang et al first described a computer-screened ACE inhibitory peptide Ile-Ala-Phe (IAF)from pumpkin seed protein. In this study, Neutrase 5.0 BG was used to hydrolyze PSM to release antihypertensive peptides which were sequentially separated by ultrafiltration (Figure ), Sephadex G-15 column chromatography (Figure ), and RP-HPLC (Figure A).…”

Section: Discussionmentioning

confidence: 99%

“…Especially, PSM contains a large amount of aromatic, hydrophobic, and alkaline amino acids which have been reported to be associated with high hypotensive activity . In addition, some existing reports have shown that the hydrolysate of PSM has hypotensive effect. − Therefore, PSM can be used as a potential resource for producing antihypertensive peptides. Further intensive research is needed to demonstrate the structure–activity relationships and to examine the underlying molecular mechanisms of the antihypertensive peptides derived from the hydrolysate of PSM.…”

Section: Introductionmentioning

confidence: 99%

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Two Novel Angiotensin-Converting Enzyme (ACE) Inhibitory and ACE2 Upregulating Peptides from the Hydrolysate of Pumpkin (Cucurbita moschata) Seed Meal

Li,

Peng,

Xiao

et al. 2024

J. Agric. Food Chem.

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Pumpkin (Cucurbita moschata) seed meal (PSM), the major byproduct of pumpkin seed oil industry, was used to prepare angiotensin-converting enzyme (ACE) inhibitory and angiotensin-converting enzyme 2 (ACE2) upregulating peptides. These peptides were isolated and purified from the PSM hydrolysate prepared using Neutrase 5.0 BG by ultrafiltration, Sephadex G-15 column chromatography, and reversed-phase high-performance liquid chromatography. Two peptides with significant ACE inhibition activity were identified as SNHANQLDFHP and PVQVLASAYR with IC 50 values of 172.07 and 90.69 μM, respectively. The C-terminal tripeptides of the two peptides contained Pro, Phe, and Tyr, respectively, and PVQVLASAYR also had Val in its Nterminal tripeptide, which was a favorable structure for ACE inhibition. Molecular docking results declared that the two peptides could interact with ACE through hydrogen bonds and hydrophobic interactions. Furthermore, the two peptides performed protective function on EA.hy926 cells by decreasing the secretion of endothelin-1, increasing the release of nitric oxide, and regulating the ACE2 activity. In vitro simulated gastrointestinal digestion showed the two peptides exhibited good stability against gastrointestinal enzyme digestion. In conclusion, PSM is a promising material for preparing antihypertensive peptides.

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“…The peptides used in the simulation were the 10 tripeptides VAP, APG, GAP, VSP, TRP, LSP, VGP, GVG, and GLG, and the three dipeptides VA, AP, and PG. The following parameters were used: Placement; Triangle Matcher; rescoring 1: London dG; Refinement: Rigid Receptor; and rescoring 2: GBVI/WSA dG [19,40,41]. The 2D interactions of peptides with ACE were shown in MOE ® 2018 [42], and the 3D docking poses were displayed in PyMOL 2.0.0a0 [7,20,37,43].…”

Section: Molecular Dockingmentioning

confidence: 99%

In Vitro and In Silico Studies on Angiotensin I-Converting Enzyme Inhibitory Peptides Found in Hydrophobic Domains of Porcine Elastin

Hatakenaka

Kato

Okamoto³

2023

Molecules

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One of the most striking aspects of the primary structure in the hydrophobic domains of the tropoelastin molecule is the occurrence of the VAPGVG repeating sequence. Since the N-terminal tripeptide VAP of VAPGVG showed a potent ACE inhibitory activity, the ACE inhibitory activity of various derivatives of VAP was examined in vitro. The results showed that VAP derivative peptides VLP, VGP, VSP, GAP, LSP, and TRP exhibited potent ACE inhibitory activities, while the non-derivative peptide APG showed only weak activity. In in silico studies, the docking score S value showed that VAP derivative peptides VLP, VGP, VSP, LSP, and TRP had stronger docking interactions than APG. Molecular docking in the ACE active pocket showed that TRP, the most potent ACE inhibitory peptide among the VAP derivatives, had a larger number of interactions with ACE residues in comparison with APG and that the TRP molecule appeared to spread widely in the ACE pocket, while the APG molecule appeared to spread closely. Differences in molecular spread may be a reason why TRP exhibits more potent ACE inhibitory activity than APG. The results suggest that the number and strength of interactions between the peptide and ACE are important for the ACE- inhibitory potency of the peptide.

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A novel Angiotensin-I-converting enzyme (ACE) inhibitory peptide IAF (Ile-Ala-Phe) from pumpkin seed proteins: in silico screening, inhibitory activity, and molecular mechanisms

Cited by 24 publications

References 37 publications

[Retracted] Exploration of ACE‐Inhibiting Peptides Encrypted in Artemisia annua Using In Silico Approach

[Retracted] Exploration of ACE‐Inhibiting Peptides Encrypted in Artemisia annua Using In Silico Approach

Two Novel Angiotensin-Converting Enzyme (ACE) Inhibitory and ACE2 Upregulating Peptides from the Hydrolysate of Pumpkin (Cucurbita moschata) Seed Meal

In Vitro and In Silico Studies on Angiotensin I-Converting Enzyme Inhibitory Peptides Found in Hydrophobic Domains of Porcine Elastin

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