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

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 α-glycosidase; the results were compared with standard compounds including acetazolamide, tacrine, and acarbose. Half maximal inhibition concentration (IC ₅₀ ) 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 IC ₅₀ value of Voriconazole was 40.77 nM for α-glycosidase, while the mean inhibition constant (K _i ) value was 17.47 ± 1.51 nM for α-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.
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