scholarly journals A UPLC-DAD-Based Bio-Screening Assay for the Evaluation of the Angiotensin Converting Enzyme Inhibitory Potential of Plant Extracts and Compounds: Pyrroquinazoline Alkaloids from Adhatoda vasica as a Case Study

Molecules ◽  
2021 ◽  
Vol 26 (22) ◽  
pp. 6971
Author(s):  
Syeda Tehreem ◽  
Saeedur Rahman ◽  
Muhammad Salman Bhatti ◽  
Reaz Uddin ◽  
Muhammad Noman Khan ◽  
...  
Keyword(s):  
Medicinal Plants ◽  
Angiotensin Converting Enzyme ◽  
Plant Extracts ◽  
Ace Inhibition ◽  
Rapid Screening ◽  
Array Detector ◽  
Converting Enzyme ◽  
Adhatoda Vasica ◽  
Standard Drug ◽  
Ace Inhibitory

Angiotensin converting enzyme (ACE) plays a crucial role in regulating blood pressure in the human body. Identification of potential ACE inhibitors from medicinal plants supported the idea of repurposing these medicinal plants against hypertension. A method based on ultra-performance liquid chromatography (UPLC) coupled with a diode array detector (DAD) was used for the rapid screening of plant extracts and purified compounds to determine their ACE inhibitory activity. Hippuryl-histidiyl-leucine (HHL) was used as a substrate, which is converted into hippuric acid (HA) by the action of ACE. A calibration curve of the substrate HHL was developed with the linear regression 0.999. The limits of detection and quantification of this method were found to be 0.134 and 0.4061 mM, respectively. Different parameters of ACE inhibitory assay were optimized, including concentration, incubation time and temperature. The ACE inhibition potential of Adhatoda vasica (methanolic-aqueous extract) and its isolated pyrroquinazoline alkaloids, vasicinol (1), vasicine (2) and vasicinone (3) was evaluated. Compounds 1–3 were characterized by various spectroscopic techniques. The IC50 values of vasicinol (1), vasicine (2) and vasicinone (3) were found to be 6.45, 2.60 and 13.49 mM, respectively. Molecular docking studies of compounds 1–3 were also performed. Among these compounds, vasicinol (1) binds as effectively as captopril, a standard drug of ACE inhibition.

scholarly journals Discovery of Novel Angiotensin-Converting Enzyme Inhibitory Peptides from Todarodes pacificus and Their Inhibitory Mechanism: In Silico and In Vitro Studies

2019 ◽  
Vol 20 (17) ◽  
pp. 4159 ◽  
Author(s):  
Dingyi Yu ◽  
Cong Wang ◽  
Yufeng Song ◽  
Junxiang Zhu ◽  
Xiaojun Zhang
Keyword(s):  
Angiotensin Converting Enzyme ◽  
In Silico ◽  
Ace Inhibition ◽  
Degree Of Hydrolysis ◽  
Converting Enzyme ◽  
Inhibitory Peptides ◽  
Todarodes Pacificus ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

In order to rapidly and efficiently excavate antihypertensive ingredients in Todarodes pacificus, its myosin heavy chain was hydrolyzed in silico and the angiotensin-converting enzyme (ACE) inhibitory peptides were predicted using integrated bioinformatics tools. The results showed the degree of hydrolysis (DH) theoretically achieved 56.8% when digested with papain, ficin, and prolyl endopeptidase (PREP), producing 126 ACE inhibitory peptides. By predicting the toxicity, allergenicity, gastrointestinal stability, and intestinal epithelial permeability, 30 peptides were finally screened, of which 21 had been reported and 9 were new. Moreover, the newly discovered peptides were synthesized to evaluate their in vitro ACE inhibition, showing Ile-Ile-Tyr and Asn-Pro-Pro-Lys had strong effects with a pIC50 of 4.58 and 4.41, respectively. Further, their interaction mechanisms and bonding configurations with ACE were explored by molecular simulation. The preferred conformation of Ile-Ile-Tyr and Asn-Pro-Pro-Lys located in ACE were successfully predicted using the appropriate docking parameters. The molecular dynamics (MD) result indicated that they bound tightly to the active site of ACE by means of coordination with Zn(II) and hydrogen bonding and hydrophobic interaction with the residues in the pockets of S1 and S2, resulting in stable complexes. In summary, this work proposed a strategy for screening and identifying antihypertensive peptides from Todarodes pacificus.

scholarly journals Extraction of Collagen from the Skin of Kacang Goat and Production of Its Hydrolysate as an Inhibitor of Angiotensin Converting Enzyme

2021 ◽  
Vol 44 (2) ◽  
pp. 222-228
Author(s):  
T. R. Hakim ◽  
A. Pratiwi ◽  
Jamhari Jamhari ◽  
N. A. Fitriyanto ◽  
Rusman Rusman ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Dry Matter ◽  
Ace Inhibition ◽  
Converting Enzyme ◽  
Inhibition Activity ◽  
Collagen Hydrolysate ◽  
Molecular Weights ◽  
Ic50 Value ◽  
Inhibitory Potential ◽  
Ace Inhibitory

The study was designed to determine the potential of collagen hydrolysate produced from the skin of Kacang goat through chymotrypsin hydrolysis to be used as an inhibitor of angiotensin converting enzyme (ACE). This research was conducted in three replications, with the measured parameters include ACE inhibitory potential and collagen hydrolysate fractionation. The results showed that collagen extraction of Kacang goat skin by chymotrypsin hydrolysis yielded 9.74% (dry matter, v/v) collagen, with pH at 6.6. The extracted collagen contained α1, α2, and β collagen chains with molecular weights of 151 kDa, 141 kDa, and 240 kDa, respectively. Furthermore, the collagen hydrolysis produced protein peptides confirmed at molecular weights of 43 to 107 kDa. The hydrolysate fractionation at molecular weights of <3 kDa, 3-5 kDa, and >5 kDa showed proteins concentrations of 2.33 mg/mL, 3.81 mg/mL, and 3.93 mg/mL, respectively. The hydrolysate fractionation with molecular weight <3 kDa showed to have ACE inhibition activity with the IC50 value of 0.47 mg/mL. The study concluded that collagen hydrolysate extracted from the skin of Kacang goat had a promising potential as a source of antihypertensive agent.

scholarly journals Plant flavonoids as angiotensin converting enzyme inhibitors in regulation of hypertension

2011 ◽  
Vol 1 (5) ◽  
pp. 172 ◽  
Author(s):  
B. W. Nileeka Balasuriya ◽  
H. P. Vasantha Rupasinghe
Keyword(s):  
Blood Pressure ◽  
Angiotensin Converting Enzyme ◽  
Enzyme Inhibition ◽  
Glucuronic Acid ◽  
Ace Inhibition ◽  
Converting Enzyme ◽  
Inhibitory Property ◽  
Ic50 Value ◽  
Ace Inhibitory

Background: Angiotensin converting enzyme (ACE) is a key component in the renin angiotensin aldosterone system (RAAS) which regulates blood pressure. As the over expression of RAAS is associated with vascular hypertension, ACE inhibition has become a major target control for hypertension. The research on potential ACE inhibitors is expanding broadly and most are focused on natural product derivatives such as peptides, polyphenolics, and terpenes. Plant polyphenolics are antioxidant molecules with various beneficial pharmacological properties. The current study is focused on investigating and reviewing the ACE inhibitory property of fruit flavonoids. An apple skin extract (ASE) rich in flavonoids, the major constituents of the extract and their selected metabolites were assessed for the ACE inhibitory property in vitro. It is important to investigate the metabolites along with the flavonoids as they are the constituents active inside the human body. Objective: To investigate whether flavonoids, flavonoid rich apple extracts and their metabolites could inhibit ACE in vitro.Method: The samples were incubated with sodium borate buffer (30 µL, pH 8.3), 150 µL of substrate (Hip-His-Liu) and ACE (30 µL) at 37 oC for 1 h. The reaction was stopped by addition of 150 µL of 0.3M NaOH. The enzyme cleaved substrate was detected by making a fluorimetric adduct by adding 100 µL of o-phthaladehyde for 10 min at room temperature. Reaction was stopped by adding 50 µL of 3M HCl. Fluorescence was measured by using a FluoStar Optima plate reader at excitation of 350 nm and emission of 500 nm. Results: The extract and the compounds showed a concentration dependant enzyme inhibition. Increasing concentrations from 0.001 ppm to 100 ppm of ASE showed an increment of 29% to 64% ACE inhibition. The IC50 (concentration of test compound which gives 50% enzyme inhibition) values of ASE, quercetin, quercetin-3-glucoside, quercetin-3-galactoside, cyanidin-3-galactoside were 49 µg/mL, 151 µM, 71 µM, 180 µM, 206 µM, respectively. The major constituents of the ASE that were tested separately showed effective ACE inhibition. From the three metabolites tested, only quercetin-3-glucuronic acid showed concentration dependant ACE inhibition. The ACE inhibition of 0.001 ppm to 100 ppm of quercetin-3-glucuronic was in the range of 43% and 75% and the IC50 value was 27 µM. Conclusion: The results demonstrated that flavonoids have a potential to inhibit ACE in vitro and the inhibitory property varies according to type of sugar moiety attached at C-3 position. The results also revealed that the major contributing compounds of ASE for ACE inhibition belong to flavonoids. Among the tested compounds, the lowest IC50 value is associated with the quercetin-3-glucuronic acid, a major in vivo metabolites of quercetin and its glycosides. The results suggest that certain dietary flavonoids may possess properties of blood pressure regulation.Key words: Hypertension, renin angiotensin system (RAS), angiotensin converting enzyme (ACE), flavonoids, apple

Angiotensin-converting enzyme (ACE)-inhibition in cirrhosis

1993 ◽  
Vol 17 (1) ◽  
pp. 40-47 ◽  
Author(s):  
V. Gross ◽  
E. Treher ◽  
K. Haag ◽  
W. Neis ◽  
U. Wiegand ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Ace Inhibition ◽  
Converting Enzyme

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.

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