In silico evaluation of molecular interactions between known α-glucosidase inhibitors and homologous α-glucosidase enzymes from Saccharomyces cerevisiae, Rattus norvegicus, and GANC-human

Abstract

The aim of this study was to observe molecular interactions between α-glucosidase inhibitor (IAG) and α-glucosidase enzymes derived from Saccharomyces cerevisiae, Rattus norvegicus, and GANC-human. These enzymes were studied against four of the well-known IAG such as 1-deoxynojirimycin, acarbose, miglitol, and voglibose. We compared the selected IAG by means of a computer-aided drug design protocol involving homology modeling of the target protein and the virtual screening with docking simulations in the binding free energy function. Compared to acarbose, miglitol, voglibose, 1-deoxynojirimycin showed a significant inhibition of three target macromolecules of α-glucosidase enzyme. 1-Deoxynojirimycin had the highest inhibition on α-glucosidase, followed by miglitol, voglibose, and acarbose, respectively.