Triazoloquinazolines as a new class of potent α-glucosidase inhibitors: in vitro evaluation and docking study

Previously, we synthesized triazoloquinazolines 1-14 and characterized their structure. In this study, we aimed to evaluate the in vitro activity of the targets 1-14 as a-glucosidase inhibitors using a-glucosidase enzyme from Saccharomyces cerevisiae type 1. Among the tested compounds, triazoloquinazolines 14, 8, 4, 5, and 3 showed the highest inhibitory activity (IC50 = 12.70 +/- 1.87, 28.54 +/- 1.22, 45.65 +/- 4.28, 72.28 +/- 4.67, and 83.87 +/- 5.12 mu M, respectively) in relation to that of acarbose (IC50 = 143.54 +/- 2.08 mu M) as a reference drug. Triazoloquinazolines were identified herein as a new class of potent a-glucosidase inhibitors. Molecular docking results envisaged the plausible binding interaction between the target triazoloquinazolines and alpha-glucosidase enzyme and indicated considerable interaction with the active site residues.