Diabetes is becoming a major threat to the world. A novel series of hybrids of coumarin-dithiocarbamate were designed and synthesized, as potential alpha-glucosidase inhibitors targeting type 2 diabetes mellitus, in excellent yield and characterized by FTIR, 1H NMR, 13C NMR. The most potent compounds 6g and 6f exhibited significant alpha-glucosidase inhibitory activity with IC50 values of 85.0 ± 4.0 μM and 101.6 ± 4.7 μM respectively. Molecular docking studies of the designed compounds against alpha-glucosidase were also carried out to compare the binding affinities with IC50 values. The predicted binding modes are in good agreement with the IC50 values and showed that the accommodation of the moiety carbamothioyl-sulfanyl at the gate area, while the coumarin moiety is involved in hydrogen bond interaction with the key amino acid His279 in the bottom of the binding site. The kinetic mechanism investigated by Lineweaver-Burk plots exhibited that compound (6g) inhibit the alpha-glucosidase enzyme competitively to form an enzyme inhibitor complex.