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Inhibition profiles of Voriconazole against acetylcholinesterase, α-glycosidase, and human carbonic anhydrase I and II isoenzymesTopal, Fevziacetylcholinesterasecarbonic anhydraseenzyme inhibitionvoriconazoleα-glycosidaseIn 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 (IC50) values were obtained from the enzyme activity (%)-[Voriconazole] graphs, whereas Ki values were calculated from the Lineweaver-Burk graphs. According to the results, the IC50 value of Voriconazole was 40.77 nM for α-glycosidase, while the mean inhibition constant (Ki) 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 Ki 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.John Wiley and Sons Inc.2019Articlehttps://rdlopen.rawdatalibrary.net/r/gumushane/12661https://doi.org/10.1002/jbt.223851095-6670enJournal of Biochemical and Molecular Toxicologyinfo:eu-repo/semantics/closedAccessinfo:eu-repo/semantics/articlehttps://gumushane-rdlopen.rawdatalibrary.net/tr/items/gumushane/12661