Erigür, Esra CanerAltuğ, CevherAngeli, AndreaSupuran, Claudiu T.2024-02-082024-02-082022Erigur, E. C., Altug, C., Angeli, A., & Supuran, C. T. (2022). Design, synthesis and human carbonic anhydrase I, II, IX and XII inhibitory properties of 1, 3-thiazole sulfonamides. Bioorganic & Medicinal Chemistry Letters, 59, 128581-128581.0960-894X1464-3405http://dx.doi.org/10.1016/j.bmcl.2022.128581https://hdl.handle.net/20.500.12491/11998We are extremely grateful to Hayat Kimya San. A S and BAIBU BAP (Project No : 2021.03.03.1499) for financial support.Carbonic anhydrases (CAs, EC 4.2.1.1) are categorized as metalloenzymes and are widespread in both eukaryotes and prokaryotes. In mammals, 16 different isoforms of carbonic anhydrase were isolated and categorized as catalytic human isoform; cytosolic CAs (CA-I, II, III, VII and XIII), membrane-associated CAs (CA-IV, IX, XII, XIV and XV), mitochondrial CAs (CA-VA and VB), secreted CAs (CA-VI) and non- catalytic human isoform; inactive CA-related proteins (CA-VIII, X, and XI).1,2 Carbonic anhydrases, which are included in the enzyme family, help to the reversible conversion of carbon dioxide and water to bicarbonate anion and proton presence of Zn2+ ion at the catalytic site. They also provide transportation of carbon dioxide (CO2), keeps acid-base balance, regulation of pH, etc.3,4 By means of their critical participation in many regulatory physiologic processes, they play an active role in the treatment of many diseases such as glaucoma, epilepsy, obesity edema, cancer, neuropathic pain, etc.5eninfo:eu-repo/semantics/closedAccessBiological EvaluationProtease InhibitorsDerivativesAnticancerTargetsVIIArticle10.1016/j.bmcl.2022.1285815914350661412-s2.0-85123370879Q2WOS:000783550500008Q2