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.
|Number of pages||7|
|Journal||Thai Journal of Pharmaceutical Sciences|
|Publication status||Published - 2018|
- Human (GANC) α-glucosidase enzyme
- Molecular docking
- Rattus norvegicus
- Saccharomyces cerevisiae