scholarly journals Identification of bioactive compounds by GC-MS and α-amylase and α-glucosidase inhibitory activity of Rauvolfia tetraphylla L. and Oroxylum indicum (L.) Kurz: an in vitro and in silico approach

2020 ◽  
Vol 6 (1) ◽  
Author(s):  
Ananta Swargiary ◽  
Manita Daimari
Keyword(s):  
Heavy Metal ◽  
Molecular Docking ◽  
Bioactive Compounds ◽  
Inhibitory Activity ◽  
In Silico ◽  
Metal Content ◽  
Leaf Extract ◽  
Oroxylum Indicum ◽  
Rauvolfia Tetraphylla

Abstract Background The practice of ethnomedicine remains to be the primary source of healthcare in many parts of the world, especially among the tribal communities. However, there is a lack of scientific outlook and investigation to authenticate and validate their medicinal values. Objective The present study investigated the trace and heavy metal content, bioactive compounds, α-amylase, and α-glucosidase inhibitory activity of Rauvolfia tetraphylla and Oroxylum indicum using in vitro and in silico methods. Methods Trace and heavy metal content of Rauvolfia tetraphylla and Oroxylum indicum were detected using Atomic Absorption Spectroscopy. Bioactive compounds were analyzed and identified by the GC-MS technique. α-Amylase and α-glucosidase inhibitory activity of the plants were studied using the spectrophotometric method using UV/VIS-Spectrophotometer. In silico molecular docking was carried out in AutoDock vina and the structures visualized using PyMol and Biovia Discovery Studio software. Statistical and graphical representations were performed using Excel and OriginPro. Results The trace and heavy metallic content such as Zn, Ni, Pb, Cr, Cu, and Mn were reported from both the plant. No Cd was detected in both the plants. GC-MS analysis revealed four major compounds in R. tetraphylla and seven in O. indicum. Biochemical studies showed that the leaf extract of O. indicum posses the strongest α-amylase and α-glucosidase inhibitory activity. R. tetraphylla showed weaker enzyme inhibition. Molecular docking study revealed that three compounds from O. indicum (O2, O3, and O6) and two from R. tetraphylla (R1 and R2) showed strong binding affinity to α-amylase and α-glucosidase. However, leaf extract of O. indicum showed better binding affinity with the enzymes compared to R. tetraphylla. Conclusion Inhibition of α-amylase and α-glucosidase in an important strategy of diabetes control. The present study revealed the in vitro α-amylase and α-glucosidase inhibitory activity of Rauvolfia tetraphylla and Oroxylum indicum. In conclusion, the study identified that the leaf extract of O. indicum as a potential inhibitor of glucose metabolizing enzymes and could be a source of antidiabetic agents.

scholarly journals Chemical Profile, Antioxidant and Alpha-Amylase Inhibitory Activity of Leaves Extracts of Annona muricata: A Combined In vitro and In silico Study

2021 ◽  
Vol 11 (2) ◽  
pp. 3470-3479
Keyword(s):  
Molecular Docking ◽  
Inhibitory Activity ◽  
In Silico ◽  
Molecular Mechanisms ◽  
Hydrophobic Interactions ◽  
In Silico Analysis ◽  
Gas Chromatography Mass Spectrometry ◽  
Annona Muricata ◽  
Butanol Extract

Leaves of Annona muricata are commonly used for treating diabetes. This study was conducted to investigate the molecular mechanisms involved in the antidiabetic properties of leaves of Annona muricata. Leaves of Annona muricata were extracted separately with H2O, hydromethanol (50% methanol), methanol, ethylacetate, and n-butanol. Chemical characterization of the extracts was performed by spectrophotometry and Gas chromatography-Mass Spectrometry (GC-MS) techniques. Biological activity was determined by α-amylase inhibition assays and molecular docking. The hydromethanol extract had a total phenolics concentration of 117.00±0.59 µg GAE/mg extract whereas; flavonoids were most abundant in the n-butanol extract accounting for 29.34±8.87 µg QE/mg extract. The n-butanol extract had the best FRAP value of 41.17±0.57 Vit C eqv mM, which was significantly higher than the value of the vitamin C reference. Estimated IC50 for all the extracts did not differ significantly but was significantly higher than the reference compound quercetin. All extracts inhibited α-amylase in vitro albeit significantly lower than acarbose. The hydromethanol extract had the highest inhibitory activity (53.31 ± 0.33%). Furthermore, chemical profiling of the hydromethanol extract revealed the presence of a variety of bioactive compounds. In silico analysis by molecular docking of the compounds identified by GC-MS on α-amylase revealed that the compounds had robust molecular interactions orchestrated by H-bonding and hydrophobic interactions. From the results, it can be concluded that extracts of Annona muricata possess antioxidant phytochemicals that inhibit α-amylase. Therefore, the results justify the use of the plant for the treatment of diabetes.

scholarly journals IN VITRO AND IN SILICO EVALUATION OF XANTHINE OXIDASE INHIBITORY ACTIVITY OF QUERCETIN CONTAINED IN SONCHUS ARVENSIS LEAF EXTRACT

2017 ◽  
Vol 10 (14) ◽  
pp. 50
Author(s):  
Rini Hendriani ◽  
Nursamsiar Nursamsiar ◽  
Ami Tjitraresmi
Keyword(s):  
Free Energy ◽  
Xanthine Oxidase ◽  
Inhibitory Activity ◽  
In Silico ◽  
Leaf Extract ◽  
Binding Free Energy ◽  
Uv Spectrophotometry ◽  
Docking Simulations ◽  
Oxidase Enzyme

Objective: The aim of the present study was to examine the inhibiting effects of quercetin contained in Sonchusarvensis leaf extract on the activity of xanthine oxidase, an essential enzyme for uric acid synthesis.Methods: Activity test was conducted in vitro by measuring the activity of xanthine oxidase using UV spectrophotometry and in silico by determining the interaction of quercetin and allopurinol (as comparation drug) with xanthine oxidase enzyme in terms of hydrogen bonds and binding free energy. Docking simulations were performed by Autodock4.2 package.Results: The active fraction, using the solvent n-hexane, ethyl acetate and water, tested the inhibitory activity of the xanthine oxidase enzyme in vitro obtained respectively IC50 of 263.19, 16.20 and 141.80 μg/ml. Isolates with highest activity identified as quercetin. The xanthine oxidase enzyme inhibitory activity insilico by molecular docking showed quercetin has free energy binding ˗7.71 kcal/mol, more negative than that of allopurinol ˗5.63 kcal/mol.Conclusion: This shows the affinity of quercetin stronger than that of allopurinol; so that it can be predicted that quercetin was more potential to inhibit xanthine oxidase enzyme activity. Thus the extract of the S. arvensis leaves containing the active compound quercetin was a potential use as antihyperuricemia.  

In-Vitro and In-Silico Alpha Glucucosidase Inhibitory activity of Oroxylum indicum

2021 ◽  
pp. 119-125
Author(s):  
Gejalakshmi S. ◽  
Harikrishnan N. ◽  
Anas S. Mohameid
Keyword(s):  
Molecular Docking ◽  
Inhibitory Activity ◽  
In Silico ◽  
Docking Study ◽  
Alpha Amylase ◽  
Scavenging Activity ◽  
Molecular Docking Study ◽  
Ic50 Value ◽  
Alpha Glucosidase

Background: Diabetes mellitus is a metabolic condition characterized by elevated blood glucose levels in the bloodstream. It occurs due to the inadequate amount of insulin secreted in the body or resistance of insulin receptors. Objective: In the present study, for its effect on alpha-amylase and alpha-glucosidase enzymes, Oroxylum indicuma flavone glycoside was assessed using in-vitro assays by removing the respective enzymes from whole wheat and barley in conjunction with in-silico analysis. Method: in-vitro alpha amylase inhibitory activity and in-vitro alpha glucosidase inhibitory activity was performed using acarbose as a standard drug. The molecular docking study was performed using Schrodinger (Maestro V 11.5) software. The parameters glide score, Lipinski rule for drug likeliness, bioactive scoring and ADME properties were assessed in the docking study. In addition, baicalein's antioxidant function was assessed using DPPH assay, nitric oxide scavenging activity. The cytotoxicity of Oroxylum indicumwas evaluated using the Brine shrimp lethality assay. Results: The alpha-amylase assay performed showed IC50 value of 48.40 µg/ml for Oroxylum indicumwhereas alpha-glucosidase assay showed an IC50 value of 16.03 µg/ml. Oroxylum indicumshows the glide score of-5.565 with 5EOF and glide score of -5.339 with 5NN8 in the molecular docking study. The highest percentage of DPPH radical scavenging activity and nitrous oxide scavenging activity were found to be.27% at160 µg/ml and 50.02% at the concentrations of 160 µg/ml respectively. Conclusion: Based on further in vivo and clinical trials, Oroxylum indicummay be used for the management of hyperglycaemia.

Evaluation of Phytopolyphenols for their gp120-CD4 Binding Inhibitory Properties by In Silico Molecular Modelling & In Vitro Cell Line Studies

2019 ◽  
Vol 17 (2) ◽  
pp. 102-113 ◽  
Author(s):  
Amit Mirani ◽  
Harish Kundaikar ◽  
Shilpa Velhal ◽  
Vainav Patel ◽  
Atmaram Bandivdekar ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Gallic Acid ◽  
Cell Line ◽  
Ellagic Acid ◽  
Inhibitory Activity ◽  
In Silico ◽  
Early Stage ◽  
Binding Mode ◽  
Hiv 1

Background:Lack of effective early-stage HIV-1 inhibitor instigated the need for screening of novel gp120-CD4 binding inhibitor. Polyphenols, a secondary metabolite derived from natural sources are reported to have broad spectrum HIV-1 inhibitory activity. However, the gp120-CD4 binding inhibitory activity of polyphenols has not been analysed in silico yet.Objectives:To establish the usage of phytopolyphenols (Theaflavin, Epigallocatechin (EGCG), Ellagic acid and Gallic acid) as early stage HIV-1 inhibitor by investigating their binding mode in reported homology of gp120-CD4 receptor complex using in silico screening studies and in vitro cell line studies.Methods:The in silico molecular docking and molecular simulation studies were performed using Schrödinger 2013-2 suite installed on Fujitsu Celsius Workstation. The in vitro cell line studies were performed in the TZM-bl cell line using MTT assay and β-galactosidase assay.Results:The results of molecular docking indicated that Theaflavin and EGCG exhibited high XP dock score with binding pose exhibiting Van der Waals interaction and hydrophobic interaction at the deeper site in the Phe43 cavity with Asp368 and Trp427. Both Theaflavin and EGCG form a stable complex with the prepared HIV-1 receptor and their binding mode interaction is within the vicinity 4 Å. Further, in vitro cell line studies also confirmed that Theaflavin (SI = 252) and EGCG (SI = 138) exert better HIV-1 inhibitory activity as compared to Ellagic acid (SI = 30) and Gallic acid (SI = 34).Conclusions:The results elucidate a possible binding mode of phytopolyphenols, which pinpoints their plausible mechanism and directs their usage as early stage HIV-1 inhibitor.

In silico and in vitro studies of the inhibitory effect of antihistamine drug Cyproheptadine hydrochloride on human salivary alpha amylase.

2020 ◽  
Vol 19 ◽  
Author(s):  
Benguechoua Madjda ◽  
Benarous Khedidja ◽  
Nia Samira ◽  
Yousfi Mohamed
Keyword(s):  
Molecular Docking ◽  
Inhibitory Activity ◽  
In Silico ◽  
Diclofenac Sodium ◽  
The Other ◽  
Alpha Amylase ◽  
Salivary Alpha Amylase ◽  
Cyproheptadine Hydrochloride ◽  
First Time

Background: For the first time, the inhibitory effects on human salivary alpha-amylase activity of the antiinflammatory drugs: indomethacin, diclofenac sodium, ketoprofen, diclofenac potassium, diclofenac, triamcinolone acetonide and the antihistamines drugs: levocetirizine dihydrochloride, desloratadine, cycloheptadine hydrochloride has been investigated to confirm the other properties of these drugs. Objective: This study aimed to determine the effect of nine known drugs on human salivary α-amylase in vitro and the nature of interactions with structure-activity relationship using molecular docking Method: The inhibition of human salivary alpha amylase by the six anti-inflammatory and three antihistamines drugs has been carried out using the new method that has been proved in our previous work. Molecular docking has been achieved for the first time for these drugs using AutoDock Vina program. Results: The Cyproheptadine hydrochloride presented the highest inhibitory activity against α-amylase with IC50=0.7 mg/ml, while the other drugs show weak activities (IC50 > 2 mg/ml). Conclusion: We conclude that Cyproheptadine hydrochloride and which studied by docking experiments exhibited the best inhibitory activity on salivary α-amylase in vitro & in silico.

scholarly journals SKRINING IN SILICO POTENSI SENYAWA ALLICIN DARI ALLIUM SATIVUM SEBAGAI ANTIPLASMODIUM

2015 ◽  
Vol 17 (2) ◽  
pp. 175-184
Author(s):  
Fatmawaty Fatmawaty ◽  
Muhammad Hanafi ◽  
Rosmalena Rosmalena ◽  
Vivitri Dewi Prasasty
Keyword(s):  
Molecular Docking ◽  
Inhibitory Activity ◽  
In Silico ◽  
Allium Sativum ◽  
Specific Interaction ◽  
Docking Analysis ◽  
Drug Candidates ◽  
In Silico Identification ◽  
Activity Mechanism

Allicin compound (2-propene-1- sulphinothioat acid S-2-propenyl ester) is known to have potential as antiplasmodium in vitro. However, the inhibitory activity mechanism of Allicin to plasmodium is still unknown. In this research, we determined the inhibitory activity of Allicin in silico. Identification of physicochemical properties of Allicin compound and two Allicin derivatives, Alc1, Alc2 and Ac2Alc3 were also conducted.. Furthermore, analysis of drug-likeness and adsorption-distribution-metabolism-excretion (ADME) were carried out on the Allicin compound and its derivatives to find the potential of these compounds as drug candidates. In determining the specific interaction, we utilized molecular docking analysis between Allicin and its derivatives against a protein target Cysteine Protease (SP). Molecular  docking results showed that Allicin derivative, Alc2 (S-prop-2-en-1-yl 3-methylbut-2-ene-1-sulfinothioate, C10H18OS2) has better potential as inhibitors than Allicin, based on the lower bond energies and the inhibition constants, thus Alc2 can be used as an antiplasmodium agent candidate.Keywords: Allicin, Allicin derivatives, drug likeness, ADME, molecular docking

scholarly journals α-Amylase Inhibitory Activity of Catunaregam spinosa (Thunb.) Tirveng.: In Vitro and In Silico Studies

2021 ◽  
Vol 2021 ◽  
pp. 1-11
Author(s):  
Deepak Timalsina ◽  
Deepti Bhusal ◽  
Hari Prasad Devkota ◽  
Krishna Prasad Pokhrel ◽  
Khaga Raj Sharma
Keyword(s):  
Molecular Docking ◽  
Ethyl Acetate ◽  
Inhibitory Activity ◽  
In Silico ◽  
Skin Diseases ◽  
Water Soluble ◽  
Gastrointestinal Problems ◽  
In Silico Studies ◽  
In Silico Molecular Docking

α-Amylase is an enzyme involved in the breaking down of large insoluble starch molecules into smaller soluble glucose molecules. Catunaregam spinosa (Thunb.) Tirveng. (syn. Randia dumetorum (Retz.) Lam., Family: Rubiaceace) has been used as traditional medicine for the treatment of gastrointestinal problems, skin diseases, and diabetes. In this context, we studied the in vitro α-amylase inhibiting properties of methanol extracts of leaves and bark of C. spinosa. The methanol extract of bark was further fractionated into hexane, dichloromethane and ethyl acetate, and water-soluble fractions, and their α-amylase inhibitory activity was evaluated. In silico molecular docking and ADMET analysis of several compounds previously reported from the bark of C. spinosa were also performed. The in vitro α-amylase inhibition activity assay of the dichloromethane fraction of extract of bark (IC50: 77.17 ± 1.75  μg/mL) was more potent as compared to hexane and ethyl acetate fractions. The in silico molecular docking study showed that previously reported compounds from the stem bark such as balanophonin, catunaregin, β-sitosterol, and medioresinol were bounded well with the active catalytic residue of porcine pancreatic α-amylase indicating better inhibition. The ADMET analysis showed the possible drug-likeness and structure-activity relationship of selected compounds. These compounds should be studied further for their potential α-amylase inhibition in animal models.

Inhibitory activity of Urena lobata leaf extract on alpha-amylase and alpha-glucosidase: in vitro and in silico approach

2021 ◽  
Vol 32 (4) ◽  
pp. 889-894
Author(s):  
Yudi Purnomo ◽  
Juliah Makdasari ◽  
Faiqoh Inayah Fatahillah
Keyword(s):  
Inhibitory Activity ◽  
In Silico ◽  
Leaf Extract ◽  
Blood Glucose Concentration ◽  
Ethanolic Extract ◽  
Docking Study ◽  
Alpha Amylase ◽  
Molecular Docking Study ◽  
Alpha Glucosidase

Abstract Objectives In food ingestion, alpha-glucosidase (α-glucosidase) and alpha-amylase (α-amylase) are enzymes that are responsible to convert a carbohydrate into glucose. Inhibition of both enzyme activities can prolong absorption of glucose in intestine and reduce post-prandial increase of blood glucose concentration, thus, it is beneficial for type-2 diabetes treatment. Traditionally, Urena lobata (U. lobata) has been used to manage diabetes, but the scientific proof of this claim remains scarce. Therefore, the objective of this study to examine the anti-diabetic potential of U. lobata leaf extract through inhibition of α-amylase and α-glucosidase. Methods U. lobata leaf extract was obtained through extraction process using ethanol and the chemical compounds in the extract were analyzed by liquid chromatography–mass spectra (LC–MS). The inhibitory activity of U. lobata on α-glucosidase and α-amylase was evaluated by in silico using docking server, whereas in vitro enzymatic assays were using para-nitrophenyl-α-d-glucopyranoside (α-NPG) and starch as substrates. The data were presented as mean ± SD and the IC50 value was calculated using SPSS. Results U. lobata leaf extract showed inhibitory activity on α-glucosidase and α-amylase with the IC50 value was 43.73 and 83.73 μg/mL, respectively, meanwhile, acarbose as standard has IC50 value at 1.14 and 0.08 μg/mL. Molecular docking study indicated β-sitosterol and stigmasterol from U. lobata extract have a huge inhibitory activity both on α-amylase and α-glucosidase based on inhibition constant (Ki) value. Conclusions Ethanolic extract of U. lobata showed inhibition activity on α-glucosidase stronger than on α-amylase as antidiabetic.

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