Synthesis, in vitro evaluation and molecular docking studies of novel triazine-triazole derivatives as potential α-glucosidase inhibitors

Wang, Guangcheng; Peng, Zhiyuan; Wang, Jing; Li, Xin; Li, Juan

doi:10.1016/j.ejmech.2016.09.067

Cited by 150 publications

(52 citation statements)

References 35 publications

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“…Docking studies were performed using Autodock Vina 21 . The centre of the grid box 26 was placed at centre_x = 12.5825, centre_y = −7.8955, centre_z = 12.5190 with dimensions size_x = 40, size_y = 40, size_z = 40. The best-scoring poses as judged by the Vina docking score were chosen and visually analysed using PyMOL 1.8.0 software ( http://www.pymol.org/ ).…”

Section: Methodsmentioning

confidence: 99%

Synthesis,in vitroinhibitory activity, kinetic study and molecular docking of novelN-alkyl–deoxynojirimycin derivatives as potential α-glucosidase inhibitors

Lin

Zeng

Chen

et al. 2020

Journal of Enzyme Inhibition and Medicinal Chemistry

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A series of novel N -alkyl-1-deoxynojirimycin derivatives 25 ∼ 44 were synthesised and evaluated for their in vitro α-glucosidase inhibitory activity to develop α-glucosidase inhibitors with high activity. All twenty compounds exhibited α-glucosidase inhibitory activity with IC 50 values ranging from 30.0 ± 0.6 µM to 2000 µM as compared to standard acarbose (IC 50 = 822.0 ± 1.5 µM). The most active compound 43 was ∼27-fold more active than acarbose. Kinetic study revealed that compounds 43 , 40 , and 34 were all competitive inhibitors on α-glucosidase with K i of 10 µM, 52 µM, and 150 µM, respectively. Molecular docking demonstrated that the high active inhibitors interacted with α-glucosidase by four types of interactions, including hydrogen bonds, π–π stacking interactions, hydrophobic interactions, and electrostatic interaction. Among all the interactions, the π–π stacking interaction and hydrogen bond played a significant role in a various range of activities of the compounds.

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Section: Methodsmentioning

confidence: 99%

Synthesis,in vitroinhibitory activity, kinetic study and molecular docking of novelN-alkyl–deoxynojirimycin derivatives as potential α-glucosidase inhibitors

Lin

Zeng

Chen

et al. 2020

Journal of Enzyme Inhibition and Medicinal Chemistry

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show abstract

“…Type 2 diabetes (T2DM) is a classic chronic metabolic disorder characterized by increased blood glucose concentration (hyperglycemia) and insulin resistance . The number of patients with diabetes in developed and developing countries has increased sharply in the last few decades, with 90–95% of them suffering from T2DM . Inhibiting starch hydrolysis to slow down the absorption of glucose in starchy foods is an effective way to prevent T2DM.…”

Section: Introductionmentioning

confidence: 99%

Inhibition of glycosidase by ursolic acid: in vitro, in vivo and in silico study

et al. 2019

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BACKGROUND: Controlling the blood glucose level is an effective method to reduce type 2 diabetes and prevent diabetes-related complications. Ursolic acid is a plant extract that can reduce postprandial hyperglycemia effectively. This study aimed to explore the inhibitory effect and interaction mechanism of ursolic acid against -amylase and -glucosidase. RESULTS: In this study, the effect of ursolic acid on glycosidase was studied in vitro, in vivo, and in silico. The half-maximal inhibitory concentration (IC 50 ) of ursolic acid on -amylase and -glucosidase was 0.482 ± 0.12 mg mL −1 and 0.213 ± 0.042 mg mL −1 , respectively. The results of enzymatic kinetics showed that ursolic acid inhibited -amylase and -glucosidase activity in a non-competitive manner. The fluorescence spectrum showed that the combination of ursolic acid and glycosidase caused the intrinsic fluorescence quenching of glycosidase. The observation of starch granules revealed that the activity of -amylase was inhibited and the hydrolysis of starch granules was prevented in the presence of ursolic acid. Molecular docking results showed that ursolic acid bound to the inactive site of -amylase and -glucosidase through the formation of ursolic acid-glucosidase complex. Ursolic acid interacted with -amylase and -glucosidase mainly through hydrogen bonding. The postprandial hypoglycemic effect of ursolic acid in C57BL/6J mice showed that the high concentration of ursolic acid could quickly reduce postprandial blood glucose level.CONCLUSION: Ursolic acid can be considered as a natural ingredient in functional foods to control postprandial blood glucose levels and prevent diabetes by delaying the digestion of starch in foods.

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“…The 3D structure of the compounds were obtained by ChemBioDraw Ultra 14.0 and ChemBio3D Ultra 14.0 softwares (CambridgeSoft, Cambridge, MA, USA). The 3D structure of α-glucosidase of Saccharomyces cerevisiae was predicted using homology modeling in our previous report [ 21 ]. The AutoDockTools 1.5.6 package was employed to generate the docking input files.…”

Section: Methodsmentioning

confidence: 99%

“…Prompted by these observations, and in continuation of our interest in the synthesis of chemically and biologically important heterocycles [ 19 , 20 , 21 , 22 ], we herein report the synthesis of a novel series of 2-substituted-4,6-diarylpyrimidine derivatives. All the synthesized compounds were tested for their in vitro α-glucosidase inhibitory activity.…”

Section: Introductionmentioning

confidence: 99%

Synthesis, Biological Evaluation and Molecular Docking Study of 2-Substituted-4,6-Diarylpyrimidines as α-Glucosidase Inhibitors

et al. 2017

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A novel series of 2-substituted-4,6-diarylpyrimidines 6a–6t has been synthesized, characterized by 1H-NMR, 13C-NMR and HRMS, and screened for in vitro α-glucosidase inhibitory activity. The majority of the screened compounds possessed significant α-glucosidase inhibitory activity with IC50 values ranging from 19.6 ± 0.21 to 38.9 ± 0.35 μM, which is more potent than the positive control α-glucosidase inhibitor acarbose (IC50 = 817.38 ± 6.27 μM). Among them, 6j was found to be the most active compound against α-glucosidase with an IC50 of 19.6 ± 0.21 μM. In addition, molecular docking studies were carried out to explore the binding interactions of 2-substituted-4,6-diarylpyrimidine derivatives with α-glucosidase.

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Synthesis, in vitro evaluation and molecular docking studies of novel triazine-triazole derivatives as potential α-glucosidase inhibitors

Cited by 150 publications

References 35 publications

Synthesis,in vitroinhibitory activity, kinetic study and molecular docking of novelN-alkyl–deoxynojirimycin derivatives as potential α-glucosidase inhibitors

Synthesis,in vitroinhibitory activity, kinetic study and molecular docking of novelN-alkyl–deoxynojirimycin derivatives as potential α-glucosidase inhibitors

Inhibition of glycosidase by ursolic acid: in vitro, in vivo and in silico study

Synthesis, Biological Evaluation and Molecular Docking Study of 2-Substituted-4,6-Diarylpyrimidines as α-Glucosidase Inhibitors

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