Carbonic anhydrase (CA) is a zinc-containing metalloenzyme that catalyses the reversible hydration of carbon dioxide to bicarbonate and proton. The human genome contains 15 isoforms of carbonic anhydrase [1]. Unlike other CA isoforms essential for cellular and tissue homeostasis, CA IX features mainly in cancer, making it an interesting target for developing new anti-cancer drugs [2]. Although a wide variety of carbonic anhydrase inhibitors is commercially available, selective inhibition of individual isoforms remains challenging due to the conservation of catalytic domain and high structural similarity among different isoforms [3]. In our study, we used computational chemistry methods to identify potential selective ligands to target CA IX specifically. We screened various small molecules against the binding site of CA IX using molecular docking and analysed the binding energies and interactions. The identified compounds have the potential to serve as lead molecules for the development of new drugs that selectively target CA IX in cancer cells.
Computational resources were provided by the e-INFRA CZ project (ID:90140), supported by the Ministry of Education, Youth and Sports of the Czech Republic. This project was supported by the grant agency of Masaryk University within programme INTERDISCIPLINARY (project id MUNI/G/1002/2021).