Background: High Blood glucose levels is one of the main problems in diabetes. α-glucosidase with decomposition of polysaccharides increases the absorption of carbohydrates from the intestine, resulting in blood glucose upsurge. Inhibition of this enzyme is one of the most important strategies for treatment of diabetes. Objective: The aim of this study was to investigate in silico inhibitory effect of flavones, found in fruit and plants, on the α-glucosidase activity. Methods: This is a descriptive-analytic approach. The structure of the flavone compounds and α-glucosidase downloaded from PubChem and PDB database respectively. Then physicochemical properties of flavone compounds were predicted by the Zink data base and Swiss ADME server. Finally, Molegro Virtual Docker 6.0 and Molecular Viewer Molegro 2.5 environments were used, to do molecular interaction among flavone compounds and the enzyme. Results: Physicochemical characteristics of investigated flavone compounds were desirable. As well all of the studied flavone compounds were able to inhibit the α-glucosidase. But among the studied compounds, luteolin and nobiletin had the lowest negative energy with 78.98 and 87.96 KJ/mole respectively, and therefore the most docking points than the miglitol (positive control). Conclusion: Examined flavone compounds in this study, mainly nobiletin, are particularly suitable because of their fine placement in the active site of the enzyme. So they have more inhibitory effect than other similar compounds. As a result, after some in vitro and in vivo, complementary studies on this compound, it is possible to distinguish it as a potent pharmaceutical inhibitor of α- glucosidase, to be used in diabetes treatment.

Background: Candida albicans is naturally present in the normal human flora. This microorganism changes into an opportunistic fungus due to imbalances in microbiome composition, especially in an impaired immune system condition. The few available antifungal classes, severe toxicity, side effects, high cost, and the emergence of drug resistance are some of the limitations that physicians have in prescribing antifungal drugs. Objective: The current research aims to study the antifungal potential of the main compounds of Cuminum cyminum L. in inhibiting secreted aspartyl proteinase of C. albicans compared to fluconazole. Methods: In silico techniques were employed in this study. The main biochemicals of C. cyminum were obtained and optimized. 2D and 3D structures of chemical compounds were retrieved from the ChemSpider database and HyperChem software respectively. Auto Dock Vina and Discovery Studio 2024 Client were done to detect the potent inhibitor against the enzyme's active site. Finally, the physicochemical and toxicity properties of inhibitors were obtained. Results: The results of Auto Dock Vina indicated that Apigenin-7-O- glucoside has 80 percent similarity with fluconazole in the potential inhibition and exhibited a high free binding energy (ΔGbind: -10.48 kcal/mol). 13 amino acid residues involved in the interaction between best ligand and receptor that are Thr221, Asp32, Asp218, Asp86, Gly34, Ile123, Tyr84, Gly85, Ile30, Ser35, Ala119, Ile216, and Lys193. Conclusion: The present study affirmed that Apigenin-7-O- glucoside in C. cyminum could be a promising inhibitor against secreted aspartyl proteinase. However, there is still a need for clinical future investigations to support these findings.