The inhibitory activity of HL-7 and HL-10 peptide from scorpion venom ( Hemiscorpius lepturus ) on angiotensin converting enzyme: Kinetic and docking study

Setayesh-Mehr, Zahra; Asoodeh, Ahmad

doi:10.1016/j.bioorg.2017.09.006

Cited by 20 publications

(6 citation statements)

References 28 publications

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“…They used molecular docking experiments using Leu-Hyp-Gly/Leu-Pro-Gly models to support these results. In other work, Setayesh-Mehr and Asoodeh [52] identified the peptides YLYELAR (HL-7) and AFPYYGHHLG (HL-10) from scorpion venom of Hemiscorpius lepturus. Authors found that these peptides are ACE inhibitors and performed docking experiments in nACE and cACE, suggesting a preference for the N domain.…”

Section: Molecular Modeling Applied To the Study Of Ace Inhibitors Inmentioning

confidence: 99%

Considerations for Docking of Selective Angiotensin-Converting Enzyme Inhibitors

Caballero

2020

Molecules

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The angiotensin-converting enzyme (ACE) is a two-domain dipeptidylcarboxypeptidase, which has a direct involvement in the control of blood pressure by performing the hydrolysis of angiotensin I to produce angiotensin II. At the same time, ACE hydrolyzes other substrates such as the vasodilator peptide bradykinin and the anti-inflammatory peptide N-acetyl-SDKP. In this sense, ACE inhibitors are bioactive substances with potential use as medicinal products for treatment or prevention of hypertension, heart failures, myocardial infarction, and other important diseases. This review examined the most recent literature reporting ACE inhibitors with the help of molecular modeling. The examples exposed here demonstrate that molecular modeling methods, including docking, molecular dynamics (MD) simulations, quantitative structure-activity relationship (QSAR), etc, are essential for a complete structural picture of the mode of action of ACE inhibitors, where molecular docking has a key role. Examples show that too many works identified ACE inhibitory activities of natural peptides and peptides obtained from hydrolysates. In addition, other works report non-peptide compounds extracted from natural sources and synthetic compounds. In all these cases, molecular docking was used to provide explanation of the chemical interactions between inhibitors and the ACE binding sites. For docking applications, most of the examples exposed here do not consider that: (i) ACE has two domains (nACE and cACE) with available X-ray structures, which are relevant for the design of selective inhibitors, and (ii) nACE and cACE binding sites have large dimensions, which leads to non-reliable solutions during docking calculations. In support of the solution of these problems, the structural information found in Protein Data Bank (PDB) was used to perform an interaction fingerprints (IFPs) analysis applied on both nACE and cACE domains. This analysis provides plots that identify the chemical interactions between ligands and both ACE binding sites, which can be used to guide docking experiments in the search of selective natural components or novel drugs. In addition, the use of hydrogen bond constraints in the S2 and S2′ subsites of nACE and cACE are suggested to guarantee that docking solutions are reliable.

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Section: Molecular Modeling Applied To the Study Of Ace Inhibitors Inmentioning

confidence: 99%

Considerations for Docking of Selective Angiotensin-Converting Enzyme Inhibitors

Caballero

2020

Molecules

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“…However, the mechanism of action of the two enzymes is different in RAS. ACE can cause an increase in blood pressure by catalyzing the reaction of the inactive angiotensin‐I to active angiotensin angiotensin‐2 (Setayesh‐Mehr & Asoodeh, 2017). On the other hand, ACE2 can enhance the body protection effect by degrading angiotensin II into angiotensin (1–7).…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of a novel angiotensin I‐converting enzyme‐inhibitory peptide derived from Alaska pollack skins

Yang

Qin

2021

Journal of Food Science

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Hydrolysates containing angiotensin I‐converting enzyme (ACE)‐inhibitory peptide were prepared from protein of Alaska pollack skins using alcalase and trypsin. The protein hydrolysate was separated by ultrafiltration, Sephadex G‐25 gel filtration chromatography and reversed phase high‐performance liquid chromatography (HPLC), from which a novel purified peptide was obtained. Both random coil structure and β‐sheet in the purified peptide were revealed in Fourier transform infrared spectrum. The amino sequence of the purified peptide was identified as GPLGVP, VLYPVK, VFLENVLR, and FEEF by HPLC‐Q‐TOF‐MS (HPLC‐quadrupole time‐of‐flight mass spectrometry). The peptide GPLGVP whose molecular weight was 538.31 Da showed the highest ACE inhibitory activity (IC50 = 105.8 µM). The purified peptide featured a noncompetitive inhibition kinetic mechanism was shown in the Lineweaver–Burk plots and was susceptible to enzymes as indicated in the studies on stability of gastrointestinal proteases. Moreover, the peptide GPLGVP can combine ACE catalytic pocket through hydrogen bonds and other forces with high binding power as disclosed in molecular docking simulation, which provides the inhibitory effect of GPLGVP on ACE.

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“…Moreover, hypertension is associated with excessive activity of the rennin-angiotensin-aldosterone system (RAAS), which plays an important role in hormone regulation or maintenance of water and electrolyte balance. The main and best-recognized enzyme in RAAS is the angiotensin-I converting enzyme (ACE), which hydrolyzes inactive angiotensin I to active vasoconstrictor angiotensin II [5]. Therefore, reduction of ACE activity in an organism is important for regulation of blood pressure and water balance.…”

Section: Introductionmentioning

confidence: 99%

The Influence of Millet Flour on Antioxidant, Anti-ACE, and Anti-Microbial Activities of Wheat Wafers

Jakubczyk

Ćwiek

Rybczyńska‐Tkaczyk

et al. 2020

Foods

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The aim of the present study was to investigate antioxidant, angiotensin converting enzyme (ACE) inhibitory, and anti-microbial activities of wheat wafers enriched with 1%, 2%, or 3% (w/w) of millet flour (M1, M2, or M3, respectively). All samples were characterized by a richer composition of protein, polyphenols, flavonoids, phenolic acids, and reducing sugar in comparison with the control sample. The highest content of the components, i.e., 1.03 mg mL−1, 0.021 mg mL−1, 2.26 mg mL−1, 0.17 µg mL−1, and 0.63 mg mL−1, respectively, was detected in sample M3. The same sample was characterized by 803.91 and 42.79% of water and oil absorption capacity, respectively. The additive did not change the rheological features of the wafers. The 3% addition of millet flour to the wafer formulation induced the highest antioxidant activity against DPPH, Fe2+ chelation, and ACE inhibitory activity of hydrolysates (IC50 = 191.04, 0.46, and 157.73 µg mL−1, respectively). The highest activities were determined in the M3 fraction <3.0 kDa (IC50 = 3.46, 0.26, and 16.27 µg mL, respectively). In turn, the M2 fraction was characterized by the highest antimicrobial activity against Listeria monocytogenes with a minimum inhibitory concentration (MIC) value of 75 µg mL−1.

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The inhibitory activity of HL-7 and HL-10 peptide from scorpion venom ( Hemiscorpius lepturus ) on angiotensin converting enzyme: Kinetic and docking study

Cited by 20 publications

References 28 publications

Considerations for Docking of Selective Angiotensin-Converting Enzyme Inhibitors

Considerations for Docking of Selective Angiotensin-Converting Enzyme Inhibitors

Purification and characterization of a novel angiotensin I‐converting enzyme‐inhibitory peptide derived from Alaska pollack skins

The Influence of Millet Flour on Antioxidant, Anti-ACE, and Anti-Microbial Activities of Wheat Wafers

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