Evaluates α-glucosidase inhibition in carbazole derivatives, suggesting potential diabetes treatment.
Introduction: One of the most prevalent metabolic illnesses is diabetes mellitus. Safer and more efficient drugs are desperately needed due to the enormous worldwide burden of diabetes. The assessment of carbazole as an antidiabetic medication is the focus of the current investigation. Materials and Methods: A library of thirteen new carbazole-schiff base derivatives was developed, examined using several spectroscopic methods, and tested against the enzyme α-glucosidase. results: All synthesized derivatives have demonstrated superior inhibitory activities (IC50 values in the range of 38.66-152.5 μM) againstα-glucosidase relative to acarbose (IC50 value of 283.7±4.808 µM) as the reference drug. Results: All synthesized derivatives have demonstrated superior inhibitory activities (IC50 values in the range of 38.66-152.5 μM) againstα-glucosidase relative to acarbose (IC50 value of 283.7±4.808 μM) as the reference drug. Discussion: The derivative bearing an aliphatic methyl group at R1 and a p-methyl group at R2 of C6 (IC50: 38.66±3.47 μM), a benzene group at R1 and a p-methyl group at R2 of C11 (IC50: 42.02±4.78 μM), and an aliphatic methyl group at R1 and a p-methoxy group at R2 of C4 (IC50: 49.73±5.38 μM) resulted in multifold potent inhibitory activities than acarbose. conclusion: Significant details on the interactions between the developed 9-ethyl-3-((E)-(((Z)-1-phenylethylidene)hydrazineylidene)methyl)-9H-carbazoles (C1-13) derivatives and α-glucosidase proteins have been obtained from the molecular docking analysis. The results may lead to novel treatment options, provide insight into the affinity for binding, and significant interaction sites for regulating postprandial glucose levels in diabetes patients. Conclusion: Significant details on the interactions between the developed 9-ethyl-3-((Z)-(((Z)-1- phenylethylidene)hydrazineylidene)methyl)-9H-carbazoles (C1-13) derivatives and α-glucosidase proteins have been obtained from the molecular docking analysis. The results may lead to novel treatment options, providing insight into binding affinity and key interaction sites for regulating postprandial glucose levels in diabetes patients.
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Sahu et al. (2026) studied this question.
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