In silico analysis and antihypertensive effect of ACE-inhibitory peptides from smooth-hound viscera protein hydrolysate: Enzyme-peptide interaction study using molecular docking simulation

Abdelhedi, Ola; Nasri, Rim; Jridi, Mourad; Mora, Leticia; Oseguera‐Toledo, Miguel E.; Aristoy, M‐Concepción; Amara, Ibtissem Ben; Nasri, Monçef

doi:10.1016/j.procbio.2017.04.032

Cited by 62 publications

(36 citation statements)

References 58 publications

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“…(f), which is the thiol group of captopril that makes pi‐sulfur interactions with the catalytic Zn 2+ ion at the active site of the enzyme. This finding is similar to that of Abdelhedi that captopril has a direct tight‐binding mutual effect on the catalytic Zn 2+ ion (interacting distance is 2.32 Å from PDB: 1UZF) deep inside the access at the active spot of the ACE, which presents ACE inhibitory activity by interacting with His383, His387 and Glu411 via basic and acidic interactions. These results may be caused by the diverse methods of molecular docking.…”

Section: Discussionsupporting

confidence: 88%

Comparison of an angiotensin‐I‐converting enzyme inhibitory peptide from tilapia (Oreochromis niloticus) with captopril: inhibition kinetics, in vivo effect, simulated gastrointestinal digestion and a molecular docking study

et al. 2019

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BACKGROUND: In order to utilize tilapia skin gelatin hydrolysate protein, which is normally discarded as industrial waste in the process of fish manufacture, we study the in vivo and in vitro angiotensin-I-converting enzyme (ACE) inhibitory activity of the peptide Leu-Ser-Gly-Tyr-Gly-Pro (LSGYGP). The aim was to provide a pharmacological basis of the development of minimal side effects of ACE inhibitors by comparative analysis with captopril in molecular docking. RESULTS:This peptide from protein-rich wastes showed excellent ACE inhibitory activity (IC 50 = 2.577 mol L −1 ) and exhibited a mixed noncompetitive inhibitory pattern with Lineweaver-Burk plots. Furthermore, LSGYGP and captopril groups both showed significant decreases in blood pressure after 6 h and maintained good digestive stability over 4 h. Molecular bond interactions differentiate competitive captopril upon hydrogen bond interactions and Zn(II) interaction. The C-terminal Pro generates three interactions (hydrogen bonds, hydrophilic interactions and Van der Waals interactions) in the peptide and effectively interactswith the S1 and S2 pockets of ACE. CONCLUSION: LSGYGP, with an IC 50 value of 2.577 mol L −1 , has an antihypertensive effect in spontaneously hypertensive rats. Through comparison with captopril, this study revealed that LSGYGP may be a potential food-derived ACE inhibitory peptide and could act as a functional food ingredient to prevent hypertension.

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Section: Discussionsupporting

confidence: 88%

Comparison of an angiotensin‐I‐converting enzyme inhibitory peptide from tilapia (Oreochromis niloticus) with captopril: inhibition kinetics, in vivo effect, simulated gastrointestinal digestion and a molecular docking study

et al. 2019

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“…ACE had a zinc ion (Zn 2+ ) in its active site that coordinates with His383, His387, and Glu411 [39][40][41]. The hydrogen bonds play an important role in binding of the inhibitors to ACE potentially [41,42]. As shown in Figure 4a, lisinopril (5362119.pdb) was docked again with ACE and the interaction mode was the same as ACE-lisinopril complex (1O86.pdb), which indicated that the molecular docking procedure by using MOE was feasible.…”

Section: Molecular Docking Simulation Between Peptide and Acementioning

confidence: 94%

“…S1 pocket includes Ala354, Glu384, and Tyr523 residues and S2 pocket includes Gln281, His353, Lys511, His513, and Tyr520 residues, while S1 contains Glu162 residue. ACE had a zinc ion (Zn 2+ ) in its active site that coordinates with His383, His387, and Glu411 [39][40][41]. The hydrogen bonds play an important role in binding of the inhibitors to ACE potentially [41,42].…”

Section: Molecular Docking Simulation Between Peptide and Acementioning

confidence: 99%

Novel ACE Inhibitory Peptides Derived from Simulated Gastrointestinal Digestion in Vitro of Sesame (Sesamum indicum L.) Protein and Molecular Docking Study

Wang

Lü

Sun

et al. 2020

IJMS

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The aim of this study was to isolate and identify angiotensin I-converting enzyme (ACE) inhibitory peptides from sesame protein through simulated gastrointestinal digestion in vitro, and to explore the underlying mechanisms by molecular docking. The sesame protein was enzymatically hydrolyzed by pepsin, trypsin, and α-chymotrypsin. The degree of hydrolysis (DH) and peptide yield increased with the increase of digest time. Moreover, ACE inhibitory activity was enhanced after digestion. The sesame protein digestive solution (SPDS) was purified by ultrafiltration through different molecular weight cut-off (MWCO) membranes and SPDS-VII (< 3 kDa) had the strongest ACE inhibition. SPDS-VII was further purified by NGC Quest™ 10 Plus Chromatography System and finally 11 peptides were identified by Nano UHPLC-ESI-MS/MS (nano ultra-high performance liquid chromatography-electrospray ionization mass spectrometry/mass spectrometry) from peak 4. The peptide GHIITVAR from 11S globulin displayed the strongest ACE inhibitory activity (IC50 = 3.60 ± 0.10 μM). Furthermore, the docking analysis revealed that the ACE inhibition of GHIITVAR was mainly attributed to forming very strong hydrogen bonds with the active sites of ACE. These results identify sesame protein as a rich source of ACE inhibitory peptides and further indicate that GHIITVAR has the potential for development of new functional foods.

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“…However, peptides presenting very diverse sequences behave as ACE inhibitors. Abdelhedia and others () showed that Pro‐Thr‐Val‐Pro‐Lys‐Arg‐Pro‐Ser‐Pro‐Thr, Pro‐Leu‐Pro‐Lys‐Arg‐Glu, Val‐Val‐Pro‐Phe‐Glu‐Gly‐Ala‐Val, and Ile‐Ala‐Gly‐Pro‐Pro‐Gly‐Ser‐Ala‐Gly‐Pro‐Ala‐Gly, peptides achieved by Esperase ® catalyzed hydrolysis of smooth‐hound viscera proteins, were capable of inhibiting ACE through a complex net of interactions involving hydrogen bonds, hydrophobic, electrostatic, and van der Waals. Other studies also suggested ACE‐inhibitory activities of peptides with a proline element at the carboxyl terminal.…”

Section: Protease Applicationsmentioning

confidence: 99%

Biotechnological Applications of Proteases in Food Technology

Tavano

Berenguer-Murcia

Secundo

et al. 2018

Comp Rev Food Sci Food Safe

235

105

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This review presents some of the hottest topics in biotechnological applications: proteases in biocatalysis. Obviously, one of the most relevant areas of application is in the hydrolysis of proteins in food technology, and that has led to a massive use on proteomics. The aim is to identify via peptide maps the different proteins obtained after a specific protease hydrolysis. However, concepts like degradomics are also taking on a more relevant importance in the use and study of proteases and will also be discussed. Other protease applications, as seem in cleaning (detergent development), the pharmaceutical industry, and in fine chemistry, will be analyzed. This review progresses from basic areas such as protease classification to a discussion of the preparation of protease-immobilized biocatalysts, considering the different problems raised by the use of immobilized proteases due to the peculiar features of the substrates, usually large macromolecules. Production of bioactive peptides via limited hydrolysis of proteins will occupy an important place in this review.

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In silico analysis and antihypertensive effect of ACE-inhibitory peptides from smooth-hound viscera protein hydrolysate: Enzyme-peptide interaction study using molecular docking simulation

Cited by 62 publications

References 58 publications

Comparison of an angiotensin‐I‐converting enzyme inhibitory peptide from tilapia (Oreochromis niloticus) with captopril: inhibition kinetics, in vivo effect, simulated gastrointestinal digestion and a molecular docking study

Comparison of an angiotensin‐I‐converting enzyme inhibitory peptide from tilapia (Oreochromis niloticus) with captopril: inhibition kinetics, in vivo effect, simulated gastrointestinal digestion and a molecular docking study

Novel ACE Inhibitory Peptides Derived from Simulated Gastrointestinal Digestion in Vitro of Sesame (Sesamum indicum L.) Protein and Molecular Docking Study

Biotechnological Applications of Proteases in Food Technology

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