Abstract

Eighteen biscoumarin analogs (1-18) were synthesized in moderately good yields and characterized by various spectroscopic methods. The biscoumarin analogs were further evaluated for α-glucosidase inhibitory potential. Amongst this series of 18 analogs, 15 analogs showed outstanding α-glucosidase inhibititory activity with IC₅₀ values ranging from  14.39 ± 0.52 to 230.22 ± 0.83 μM when compared with the standard acarbose of  IC₅₀ value of 774.5 ± 1.94 μM, in which analog 4 was observed as the most active analog. Molecular docking study was carried out to understand the binding interaction of the compounds with the active site of α-glucosidase. Analog 4 was found to possess the most interaction with various proteins. This is in line with the findings in the α-glucosidase assay.