Saeedeh Rahnama Falavarjani, Azizeh Asadzadeh, Fatemeh Heidarian Naini,
Volume 18, Issue 1 (1-2019)
Abstract
Background: Inhibitors of α-glucosidase by interfering with digestion of carbohydrates play a role in controlling diabetes. Thymus vulgaris is an herb belonging to the mint family (lamiaceae). The essence of this plant contain the phenols such as thymol and carvacrol, cymene, linalool, pinene. The aim of this study was to investigate the inhibitory effect of the constituents of the thymus vulgaris extract on the activity of α-glucosidase enzyme by molecular docking.
Methods: In this study, to investigate how the compounds are attached to the active site of the enzyme, mapping of chemical structure of the compounds, energy optimization, docking studies and final analysis were carried out by ChemDraw, HyperChem, AutoDock 4.2, DS Visualizer and Lig Pluto software, respectively.
Results: All of the studied compounds were able to occupy the active site of the enzyme, among all of them, the best results of docking was related to the combination of Caryophlla-4- (12), 8 (13) -dien-5-β-ol. In fact, this compound has the most negative energy level of connection, the highest affinity for binding to the active site of the enzyme and the interaction site is similar to that of the co-crystal molecule.
Conclusion: considering the high efficacy of plant extract compounds in the bioinformatics study, and for complementary studies, the effect of the extract of this plant can be analyzed in order to control the increase of glucose in vitro and in vivo conditions.
Morteza Sadeghi, Mehran Miroliaei,
Volume 20, Issue 3 (2-2021)
Abstract
Background: Diabetes mellitus is a metabolic syndrome characterized by elevated blood glucose. The α-glucosidase enzymes that are found in the small intestine are responsible for the hydrolysis of carbohydrates. The aim of this study was to Bioinformatics evaluation of T.foenum active compounds in suppression of α-glucosidase enzyme.
Methods: This study was a descriptive-analytical method. For this purpose, the compounds separation of Trigonella foenum were first downloaded from PubChem database and then the α-glucosidase enzyme file was obtained from PDB database. The toxicity class of compounds and the Lipinski rules were predicted by Toxtree & Protox II and the Swiss ADME server, respectively. Finally, molecular docking and enzyme interaction with the compounds in Trigonella foenumwere performed by AutoDock Tools 1.5.6 and Molegro Virtual Docker 6.0. Interaction results were also analyzed using Discovery Studio 3.5 & Ligplot 2.1 software.
Results: The results indicated that all selected of compounds in Trigonella foenumwere in follow with Lipinski's rules, proper binding energy, and lack of toxicity were appropriate options for α-glucosidase inhibition. But among these compounds, Vitexin had the lowest binding energy and the most inhibitory effect on the α-glucosidase enzyme, with -4.8 kcal/mol. These compounds also had lower binding energy than standard inhibitor (Voglibose).
Conclusion: From the results of this study, it can be concluded that among the most important compounds in Trigonella foenum, the Vitexin compound power inhibitor that due to more hydrogen and hydrophobic interactions with the α-glucosidase enzyme active site.
