scholarly journals Angiotensin Converting Enzyme (ACE)-Peptide Interactions: Inhibition Kinetics, In Silico Molecular Docking and Stability Study of Three Novel Peptides Generated from Palm Kernel Cake Proteins

Biomolecules ◽  
2019 ◽  
Vol 9 (10) ◽  
pp. 569 ◽  
Author(s):  
Mohammad Zarei ◽  
Najib Abidin ◽  
Shehu Auwal ◽  
Shyan Chay ◽  
Zaibunnisa Abdul Haiyee ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Angiotensin Converting Enzyme ◽  
Inhibitory Activity ◽  
Palm Kernel ◽  
Stability Study ◽  
Converting Enzyme ◽  
Palm Kernel Cake ◽  
Inhibition Kinetics ◽  
Ace Inhibitory Activity ◽  
Ace Inhibitory

Three novel peptide sequences identified from palm kernel cake (PKC) generated protein hydrolysate including YLLLK, WAFS and GVQEGAGHYALL were used for stability study against angiotensin-converting enzyme (ACE), ACE-inhibition kinetics and molecular docking studies. Results showed that the peptides were degraded at different cleavage degrees of 94%, 67% and 97% for YLLLK, WAFS and GVQEGAGHYALL, respectively, after 3 h of incubation with ACE. YLLLK was found to be the least stable (decreased ACE-inhibitory activity) compared to WAFS and GVQEGAGHYALL (increased ACE-inhibitory activity). YLLLK showed the lowest Ki (1.51 mM) in inhibition kinetics study when compared to WAFS and GVQEGAGHYALL with Ki of 2 mM and 3.18 mM, respectively. In addition, ACE revealed the lowest K m app and V max app and higher catalytic efficiency (CE) in the presence of YLLLK at different concentrations, implying that the enzyme catalysis decreased and hence the inhibition mode increased. Furthermore, YLLLK showed the lowest docking score of −8.224 and seven interactions with tACE, while peptide GVQEGAGHYALL showed the higher docking score of −7.006 and five interactions with tACE.

scholarly journals Angiotensin-converting enzyme (ACE) inhibitory activity of Solanum torvum and isolation of a novel methyl salicylate glycoside

2014 ◽  
Vol 11 ◽  
pp. 557-562 ◽  
Author(s):  
Arunee Simaratanamongkol ◽  
Kaoru Umehara ◽  
Hiroki Niki ◽  
Hiroshi Noguchi ◽  
Pharkphoom Panichayupakaranant
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Inhibitory Activity ◽  
Methyl Salicylate ◽  
Converting Enzyme ◽  
Ace Inhibitory Activity ◽  
Solanum Torvum ◽  
Ace Inhibitory

scholarly journals ANGIOTENSIN CONVERTING ENZYME INHIBITORY ACTIVITY OF MELINJO (GNETUM GNEMON L.) SEED EXTRACTS AND MOLECULAR DOCKING OF ITS STILBENE CONSTITUENTS

2017 ◽  
Vol 10 (3) ◽  
pp. 243
Author(s):  
Abdul Mun'im ◽  
Muhammad Ashar Munadhil ◽  
Nuraini Puspitasari ◽  
Azminah . ◽  
Arry Yanuar
Keyword(s):  
Molecular Docking ◽  
Angiotensin Converting Enzyme ◽  
Ethyl Acetate ◽  
Inhibitory Activity ◽  
Phenolic Content ◽  
Ethyl Acetate Extract ◽  
Total Phenolic ◽  
Converting Enzyme ◽  
Gnetum Gnemon ◽  
Ace Inhibitory

ABSTRACTObjectives: To evaluate the angiotensin converting enzyme (ACE) inhibitory activity of melinjo (Gnetum gnemon) seed extract and to study moleculardocking of stilbene contained in melinjo seeds.Methods: Melinjo seed powders were extracted with n-hexane, dichloromethane, ethyl acetate, methanol, and water successively. The extracts wereevaluated ACE inhibitory activities using ACE kit-Wist and the phenolic content using Folin–Ciocalteu method. The extract demonstrated the highestACE inhibitory activity was subjected to liquid chromatography-mass spectrometry (LC-MS) to know its stilbene constituent. The stilbene constituentsin melinjo seed were performed molecular docking using AutoDock Vina, and ligand-receptor Interactions were processed using Ligand Scout.Results: The ethyl acetate extract demonstrated the highest ACE inhibition activity with inhibitory concentration 50% value of 9.77 × 10−8 μg/mLand the highest total phenolic content (575.9 mg gallic acid equivalent/g). Ultra-performance LC-MS analysis of ethyl acetate extract has detected theexistency of resveratrol, gnetin C, ε-viniferin, and gnemonoside A/B. These compounds displayed similar physiochemical properties to lisinopril (ACEinhibitor), as in silico molecular docking studies demonstrated that they fit into the lisinopril receptors.Conclusion: In vitro analysis ethyl acetate extract from melinjo seeds demonstrated the highest ACE inhibitory activity. Molecular docking analysisindicated that resveratrol dimers, gnetin C and gnemonoside A can be considered ACE inhibitor.Keywords: Angiotensin converting enzyme inhibitor, Gnetum gnemon, Melinjo, Total phenolic, Antihypertension, Molecular docking.

scholarly journals The Potential Angiotensin-Converting Enzyme Inhibitory Activity of Oleanolic Acid in the Hydroethanolic Extract of Crataegus monogyna Jacq

2006 ◽  
Vol 1 (5) ◽  
pp. 1934578X0600100 ◽  
Author(s):  
Everaldo Attard ◽  
Henrietta Attard
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Oleanolic Acid ◽  
Inhibitory Activity ◽  
Acid Group ◽  
Converting Enzyme ◽  
Ace Inhibitory Activity ◽  
Crataegus Monogyna ◽  
Triterpenic Acids ◽  
Hydroethanolic Extract ◽  
Ace Inhibitory

The hydroethanolic extract of Crataegus monogyna was studied for its chemical constitution and angiotensin-converting enzyme (ACE) inhibitory activity. The extract contained triterpenic acids, flavonoids and coumarins. The ACE inhibitory activity was studied using captropril, as a control drug, and oleanolic acid, as a constituent of the hydroethanolic extract and a member of the triterpenic acid group. The hydroethanolic extract and oleanolic acid showed higher IC50 values (335.00 μg/mL and 3.61 μM, respectively) in comparison to captopril (46.9 nM). However, these results indicate the anti-ACE activity of oleanolic acid and the triterpenic acids, which has not been demonstrated earlier for hawthorn extracts. In previous studies, the ACE inhibitory activity of C. monogyna extracts was always attributed to flavonoids and proanthocyanidins.

The synthesis and Angiotensin Converting Enzyme (ACE) inhibitory activity of chalcones and their pyrazole derivatives

2010 ◽  
Vol 20 (6) ◽  
pp. 1990-1993 ◽  
Author(s):  
Marco Bonesi ◽  
Monica R. Loizzo ◽  
Giancarlo A. Statti ◽  
Sylvie Michel ◽  
François Tillequin ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Inhibitory Activity ◽  
Pyrazole Derivatives ◽  
Converting Enzyme ◽  
Ace Inhibitory Activity ◽  
Ace Inhibitory

scholarly journals Identification and Molecular Docking Study of a Novel Angiotensin-I Converting Enzyme Inhibitory Peptide Derived from Enzymatic Hydrolysates of Cyclina sinensis

Marine Drugs ◽  
2018 ◽  
Vol 16 (11) ◽  
pp. 411 ◽  
Author(s):  
Fangmiao Yu ◽  
Zhuangwei Zhang ◽  
Liwang Luo ◽  
Junxiang Zhu ◽  
Fangfang Huang ◽  
...  
Keyword(s):  
Liquid Chromatography ◽  
Molecular Docking ◽  
Inhibitory Activity ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptide ◽  
Angiotensin I Converting Enzyme ◽  
Cyclina Sinensis ◽  
Ace Inhibitory

Marine-derived angiotensin-I converting enzyme (ACE) inhibitory peptides have shown potent ACE inhibitory activity with no side effects. In this study, we reported the discovery of a novel ACE-inhibitory peptide derived from trypsin hydrolysates of Cyclina sinensis (CSH). CSH was separated into four different molecular weight (MW) fractions by ultrafiltration. Fraction CSH-I showed the strongest ACE inhibitory activity. A peptide was purified by fast protein liquid chromatography (FPLC) and reversed-phase high-performance liquid chromatography (RP-HPLC) and its sequence was determined to be Trp-Pro-Met-Gly-Phe (WPMGF, 636.75 Da). The Lineweaver-Burk plot showed that WPMGF was a competitive inhibitor of ACE. WPMGF showed a significant degree of stability at varying temperatures, pH, and simulated gastrointestinal environment conditions. We investigated the interaction between this pentapeptide and ACE by means of a flexible molecular docking tool. The results revealed that effective interaction between WPMGF and ACE occurred mainly through hydrogen bonding, hydrophobic interactions, and coordination bonds between WPMGF and Zn(II). In conclusion, our study indicates that a purified extract derived from Cyclina sinensis or the WPMGF peptide could potentially be incorporated in antihypertensive functional foods or dietary supplements.

Insects as source of angiotensin converting enzyme inhibitory peptides

2017 ◽  
Vol 3 (4) ◽  
pp. 231-240 ◽  
Author(s):  
A. Cito ◽  
M. Botta ◽  
V. Francardi ◽  
E. Dreassi
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Inhibitory Activity ◽  
Bioactive Peptides ◽  
Hypertension Treatment ◽  
Converting Enzyme ◽  
Oecophylla Smaragdina ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

Hypertension is well known as one of the major risk for cardiovascular diseases which annually affect millions of people. The angiotensin converting enzyme (ACE) plays a key role in blood pressure regulation process. Indeed, hypertension treatment by synthetic ACE inhibitors (e.g. captopril, lisinopril and ramipril) is effective; however, their use can cause serious side effects, such as hypotension, cough, reduced renal function and angioedema. Thus, research was focused on natural ACE inhibitory peptides sources such as foodstuffs and also, more recently, edible insects. In the last decades, ACE inhibitory activity has been detected in protein hydrolysates from insect species belonging to the orders of Coleoptera, Diptera, Hymenoptera, Lepidoptera and also Orthoptera. Further investigations led to identify specific ACE inhibitory peptides from the silkworm Bombyx mori (Lepidoptera: Bombycidae), the yellow mealworm Tenebrio molitor (Coleoptera: Tenebrionidae), the cotton leafworm Spodoptera littoralis (Lepidoptera: Noctuidae) and also from the weaver ant Oecophylla smaragdina (Hymenoptera: Formicidae). Even if ACE inhibitory activity of these bioactive peptides has been in vitro assayed and is comparable to those of some bioactive peptides derived from other animal protein sources, the in vivo effectiveness of most of these bioactive peptides still needs to be confirmed. The aim of this review is to present an outline of the currently available data on the potential use of insects for hypertension treatment with a focus on the ACE inhibitory peptides identified in these invertebrates to date.

scholarly journals Bioactive properties of protein hydrolysate of cottonseed byproduct: antioxidant, antimicrobial, and angiotensin‐converting enzyme (ACE) inhibitory activity

2020 ◽  
Vol 34 (S1) ◽  
pp. 1-1
Author(s):  
Mariana Buranelo Egea ◽  
Josemar Gonçalves de Oliveira Filho ◽  
Ailton Cesar Lemes ◽  
Erika Valencia-Mejia ◽  
Katia Flavia Fernandes ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Inhibitory Activity ◽  
Protein Hydrolysate ◽  
Converting Enzyme ◽  
Ace Inhibitory Activity ◽  
Bioactive Properties ◽  
Ace Inhibitory
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