The molecular mechanisms of interactions between bioactive peptides and angiotensin-converting enzyme

Pan, Daodong; Guo, Huiqing; Zhao, Bo; Cao, Jinxuan

doi:10.1016/j.bmcl.2011.05.033

Cited by 32 publications

(26 citation statements)

References 26 publications

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“…In addition, these peptides formed a number of favorable salt bridge interactions with ACE residues, indicating that the ligands can pack tightly into the binding site and effectively inhibit ACE. Furthermore, it is interesting to note that hydrophobic amino acid residues such as proline, leucine, and isoleucine were mainly involved in establishing strong interactions with ACE, which goes in accordance with what is reported in SAR (Tables 1-4) [33].…”

Section: Discussionsupporting

confidence: 87%

“…Some studies have indicated that tri-peptides show higher ACE-inhibitory activity, and the C terminus end of the tri-peptides substantially affects binding to ACE. Hydrophobic amino acid residues or Proline residues at the carboxyl end are important for ACE inhibition and inhibitors containing these residues are resistant to digestion [33].…”

Section: Introductionmentioning

confidence: 99%

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Whey-Derived Peptides Interactions with ACE by Molecular Docking as a Potential Predictive Tool of Natural ACE Inhibitors

Chamata

Watson

Jauregi

2020

IJMS

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Several milk/whey derived peptides possess high in vitro angiotensin I-converting enzyme (ACE) inhibitory activity. However, in some cases, poor correlation between the in vitro ACE inhibitory activity and the in vivo antihypertensive activity has been observed. The aim of this study is to gain insight into the structure-activity relationship of peptide sequences present in whey/milk protein hydrolysates with high ACE inhibitory activity, which could lead to a better understanding and prediction of their in vivo antihypertensive activity. The potential interactions between peptides produced from whey proteins, previously reported as high ACE inhibitors such as IPP, LIVTQ, IIAE, LVYPFP, and human ACE were assessed using a molecular docking approach. The results show that peptides IIAE, LIVTQ, and LVYPFP formed strong H bonds with the amino acids Gln 259, His 331, and Thr 358 in the active site of the human ACE. Interestingly, the same residues were found to form strong hydrogen bonds with the ACE inhibitory drug Sampatrilat. Furthermore, peptides IIAE and LVYPFP interacted with the amino acid residues Gln 259 and His 331, respectively, also in common with other ACE-inhibitory drugs such as Captopril, Lisinopril and Elanapril. Additionally, IIAE interacted with the amino acid residue Asp 140 in common with Lisinopril, and LIVTQ interacted with Ala 332 in common with both Lisinopril and Elanapril. The peptides produced naturally from whey by enzymatic hydrolysis interacted with residues of the human ACE in common with potent ACE-inhibitory drugs which suggests that these natural peptides may be potent ACE inhibitors.

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Section: Discussionsupporting

confidence: 87%

Section: Introductionmentioning

confidence: 99%

Whey-Derived Peptides Interactions with ACE by Molecular Docking as a Potential Predictive Tool of Natural ACE Inhibitors

Chamata

Watson

Jauregi

2020

IJMS

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“…B). The lower activity in the other fractions may have resulted from the nature and amino acid composition of peptides that could not efficiently bind to the active site of ACE and thereby hinder the enzyme activity . Therefore, peptides from RP‐HPLC fraction IV, which showed potent ACE inhibition, were further purified to obtain a single peak (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Due to the fact that each fraction of RP‐HPLC still contained a mixture of many peptides, the predicted peptides obtained from LC‐MS/MS were analyzed for their ability to bind to the active site of ACE . The structure of peptides were docked into the active site in a docking box of 50 × 78× 60 Å using Autodock V.4 (Molecular Graphic Laboratory, Scripps Research Institute, CA, USA).…”

Section: Methodsmentioning

confidence: 99%

Angiotensin‐converting enzyme inhibitory and antioxidant peptides from digestion of larvae and pupae of Asian weaver ant, Oecophylla smaragdina, Fabricius

et al. 2017

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“…In terms of P2, the docking study showed that it formed hydrogen bonds with His353, His513 and Thr282, suggesting that P2 was involved in S2 active site pocket of ACE ( Figure 6(b)). It was found that a traditional drug of Lisinopril combined with Ala354, His353 and Glu384, and also can be direct connect with the Zn(II) of ACE [32]. ACEinhibitory peptides exerted a relatively low activity in comparison with medicinal products, but dramatically alleviate side-effects.…”

Section: Molecular Dockingmentioning

confidence: 99%

Collaborative optimization and molecular docking exploration of novel ACE-inhibitory peptides from bovine milk by complex proteases hydrolysis

Chen

Shangguan

Bao

et al. 2019

Artificial Cells, Nanomedicine, and Biotechnology

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Food-originated angiotensin-I-converting enzyme (ACE)-inhibitory peptides to preserve hypertension are widely investigated over the past decade. Our research aims to discovery novel ACE-inhibitory peptides from bovine milk by couple of complex proteases (alcalase and protease). By means of response surface methodology with the conditions of pH 9.01, 61.81 C and 6.5% ratio of enzyme to substrate, the hydrolysis model contributes to best-performing ACE-inhibitory activity of 85.02%. Through the further purification by consequent ultrafiltration, macroporous resin and gel chromatography, fraction G 2-2 is eventually obtained with ACE-inhibitory activity as high as 92.7%. Two novel peptides of VLPVPQ and VAPFPE are identified by Q-Exactive LC-MS/MS. The molecular docking study further suggests that two novel peptides have good combinations of the S1 and S2 active site pockets and Zn(II) of ACE. Our study provides a fitted mathematical model to produce two novel milk-derived ACE-inhibitory peptides, potentially developing the functional foods, especially for hypertension therapy as initial treatment.

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The molecular mechanisms of interactions between bioactive peptides and angiotensin-converting enzyme

Cited by 32 publications

References 26 publications

Whey-Derived Peptides Interactions with ACE by Molecular Docking as a Potential Predictive Tool of Natural ACE Inhibitors

Whey-Derived Peptides Interactions with ACE by Molecular Docking as a Potential Predictive Tool of Natural ACE Inhibitors

Angiotensin‐converting enzyme inhibitory and antioxidant peptides from digestion of larvae and pupae of Asian weaver ant, Oecophylla smaragdina, Fabricius

Collaborative optimization and molecular docking exploration of novel ACE-inhibitory peptides from bovine milk by complex proteases hydrolysis

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