Evaluation of effects of some coumarin metal complexes on alpha-glucosidase enzyme

α-glucosidase inhibitors (AGIs) are a class of drugs that work by inhibiting the enzyme α-glucosidase, which breaks down complex carbohydrates into simple sugars in the small intestine. By blocking this process, AGIs can slow down the absorption of carbohydrates, resulting in a smaller rise in blood glucose levels after meals. This makes them particularly useful in the management of type 2 diabetes, where hyperglycemia after meals is a common problem. In recent years, there has been a growing interest in the development of new AGIs with improved potency and selectivity, as well as better pharmacokinetic properties. These new compounds are often designed based on the structure-activity relationships of existing AGIs, and various synthetic strategies are employed to optimize their pharmacological properties. Docking experiments were performed on the crystal structure α-glucosidase. In this study, ten complexes were used, and one of these complexes. The Pd(3MeOCTS)2 inhibited the α-glucosidase enzyme, to put it another way. At an MolDock Score value of -144.099, Pd(3MeOCTS)2 was shown to inhibit the α-glucosidase enzyme, and 3D interaction maps between the two were shown.