Theses (MSc. Analytical & Pharmaceutical Chemistry)

α-Glucosidase is an intestinal membrane-bound enzyme that catalyze the final step in the digestion of carbohydrates. It cleaves the glycosidic bond of the oligosaccharides to release glucose and its inhibition results in a delayed glucose absorption and thereby inhibiting postprandial hyperglycemia and hyperinsulinemia in type 2 diabetic patients. Therefore, in view of the biological role of α-glucosidase as antidiabetic drug target, a series of six 5-(substituted)-1,3-thiazolidine-2,4-diones have been designed, synthesised and characterised by FT-IR, 1H NMR, 13C NMR and mass spectral analyses. All the compounds were subjected to the in vitro α-glucosidase inhibitory potential. Molecular docking studies have also been performed using the Schrödinger software “Glide module”. All compounds tested for the α- glucosidase inhibitory potential and all compounds exhibited significant inhibitions at IC50 values ranging from 0.0400 ± 0.3206 to 2.6847 ± 3.1441μM. Based on the molecular docking study, the binding properties (binding energy, binding orientation and binding interaction) of the ligandsrevealed the positive contribution of the 1,3-thiazolidine-2,4-dione moiety and phenyl ring substituents substituted at position 5 of 1,3-thiazolidine-2,4-dione towards the observed activity. Keywords: 5-(substituted)-1,3-thiazolidine-2,4-diones, α-glucosidase inhibitors, molecular docking