In silico prediction suggests inhibitory effect of halogenated boroxine on human catalase and carbonic anhydrase

Tarik Corbo; Abdurahim Kalajdzic; Dzelila Delic; Sumaia Suleiman; Naris Pojskic

doi:10.1186/s43141-022-00437-x

In silico prediction suggests inhibitory effect of halogenated boroxine on human catalase and carbonic anhydrase

J Genet Eng Biotechnol. 2022 Nov 3;20(1):153. doi: 10.1186/s43141-022-00437-x.

Authors

Tarik Corbo¹, Abdurahim Kalajdzic², Dzelila Delic³, Sumaia Suleiman³, Naris Pojskic²

Affiliations

¹ Institute for Genetic Engineering and Biotechnology, University of Sarajevo, Zmaja od Bosne 8, 71000, Sarajevo, Bosnia and Herzegovina. tarik.corbo@ingeb.unsa.ba.
² Institute for Genetic Engineering and Biotechnology, University of Sarajevo, Zmaja od Bosne 8, 71000, Sarajevo, Bosnia and Herzegovina.
³ Faculty of Science, University of Sarajevo, Zmaja od Bosne 33 - 35, 71000, Sarajevo, Bosnia and Herzegovina.

Abstract

Background: This research work included bioinformatics modeling of the dipotassium-trioxohydroxytetrafluorotriborate-halogenated boroxine molecule, as well as simulation and prediction of structural interactions between the halogenated boroxine molecule, human carbonic anhydrase, and human catalase structures. Using computational methods, we tried to confirm the inhibitory effect of halogenated boroxine on the active sites of these previously mentioned enzymes. The three-dimensional crystal structures of human catalase (PDB ID: 1DGB) and human carbonic anhydrase (PDB ID: 6FE2) were retrieved from RCSB Protein Data Bank and the protein preparation was performed using AutoDock Tools. ACD/ChemSketch and ChemDoodle were used for creating the three-dimensional structure of halogenated boroxine. Molecular docking was performed using AutoDock Vina, while the results were visualized using PyMOL.

Results: Results obtained in this research are showing evidence that there are interactions between the halogenated boroxine molecule and both previously mentioned proteins (human carbonic anhydrase and human catalase) in their active sites, which led us to the conclusion that the inhibitory function of halogenated boroxine has been confirmed.

Conclusion: These findings could be an important step in determining the exact mechanisms of inhibitory activity and will hopefully serve in further research purposes of complex pharmacogenomics studies.

Keywords: Dipotassium-trioxohydroxytetrafluorotriborate; Halogenated boroxine; Human carbonic anhydrase; Human catalase; In silico; Inhibitory.