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Inhibition profiles of Voriconazole against acetylcholinesterase, α‐glycosidase, and human carbonic anhydrase I and II isoenzymes
Author(s) -
Topal Fevzi
Publication year - 2019
Publication title -
journal of biochemical and molecular toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.526
H-Index - 58
eISSN - 1099-0461
pISSN - 1095-6670
DOI - 10.1002/jbt.22385
Subject(s) - chemistry , voriconazole , carbonic anhydrase , acetazolamide , acetylcholinesterase , isozyme , enzyme , tacrine , carbonic anhydrase i , ic50 , enzyme kinetics , aché , biochemistry , stereochemistry , pharmacology , active site , in vitro , medicine , biology , microbiology and biotechnology , antifungal
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.