Akademik Veri Yönetim Sistemi
13th Conference on Carbonic Anhydrases (ICCA 2025) , Sevilla, İspanya, 2 - 04 Nisan 2025, ss.59, (Özet Bildiri)
Carbonic anhydrase (CA) enzymes catalyze the reversible hydration of CO₂ into bicarbonate and protons.1 In humans, CA IX and CA XII play crucial roles in tumor progression, especially under hypoxia, which induces their overexpression. Sulfonamides, a well-studied class of CA inhibitors, function by binding to the enzyme's zinc ion, blocking its activity.2 Thiosemicarbazone derivatives have demonstrated selective cytotoxicity against cancer cells while sparing normal cells, making them highly desirable in cancer treatment.3 Heterocyclic compounds, including pyridine, pyrimidine, and 1,2,3-triazole scaffolds, along with sulfonamide functions, exhibit both anticancer activity and human carbonic anhydrase (hCA) inhibition.4 Among them, 1,2,3-triazole derivatives stand out due to their stability against metabolic degradation, hydrogen bonding potential, and enhanced solubility, making them effective in binding biomolecular targets. Although not naturally occurring, synthetic molecules containing 1,2,3-triazole units display diverse biological activities.5 Sulfonamide derivatives incorporating 1,2,3-triazole moieties, either as linkers or tail groups, have demonstrated potent and selective inhibition of specific hCA isoforms, reinforcing their significance in drug development.6 In light of this information, novel benzenesulfonamides containing 1,2,3-triazole moieties were synthesized via a cycloaddition reaction. These compounds were then coupled with N-(4-sulfamoylphenyl)hydrazinecarbothioamide to obtain new derivatives. Their structures were confirmed through various spectral and elemental analysis methods. The synthesized compounds were evaluated for their inhibitory activity against hCA I, II, IX, and XII, with some demonstrating potent inhibition, showing competitive Ki values compared to acetazolamide.