Inhibition profiles of Voriconazole against acetylcholinesterase, alpha-glycosidase, and human carbonic anhydrase I and II isoenzymes

Abstract

In this work, the inhibitory activity of Voriconazole was measured against some metabolic enzymes, including human carbonic anhydrase (hCA) I and II isoenzymes, acetylcholinesterase (AChE), and alpha-glycosidase; the results were compared with standard compounds including acetazolamide, tacrine, and acarbose. Half maximal inhibition concentration (IC50) values were obtained from the enzyme activity (%)-[Voriconazole] graphs, whereas K-i values were calculated from the Lineweaver-Burk graphs. According to the results, the IC50 value of Voriconazole was 40.77 nM for alpha-glycosidase, while the mean inhibition constant (K-i) value was 17.47 +/- 1.51 nM for alpha-glycosidase. The results make an important contribution to drug design and have pharmacological applications. In addition, the Voriconazole compound demonstrated excellent inhibitory effects against AChE and hCA isoforms I and II. Voriconazole had K-i values of 29.13 +/- 3.57 nM against hCA I, 15.92 +/- 1.90 nM against hCA II, and 10.50 +/- 2.46 nM against AChE.