Inhibition of the b-carbonic anhydrase (CA, EC 4.2.1.1) from pathogenic Candida glabrata (CgNce103) by 1H-indole-2,3-dione 3-[N-(4-sulfamoylphenyl)thiosemicarbazones] 4a–m was investigated. All the compounds were found to be potent inhibitors of CgNce103, with inhibition constants in the range of 6.4- 63.9 nM. The 5,7-dichloro substituted derivative 4l showed the most effective inhibition (KI of 6.4 nM) as well as the highest selectivity for inhibiting CgNce103 over the cytosolic human (h) isoforms hCA I and II. A possible binding interaction of compound 4l within the active site of CgNce103 has been proposed based on docking studies.Akdemir, ATİLLAANGELI, AGÖKTAŞ, FEraslan, ElmaKARALı, NSUPURAN, CT2019-10-052019-10-052019-12-01Akdemir A., ANGELI A., GÖKTAŞ F., Eraslan E., KARALı N., SUPURAN C., -Novel 2-indolinones containing a sulfonamide moiety as selective inhibitors of candida β-carbonic anhydrase enzyme.-, Journal of enzyme inhibition and medicinal chemistry, cilt.34, ss.528-531, 2019https://hdl.handle.net/20.500.12645/3777Inhibition of the b-carbonic anhydrase (CA, EC 4.2.1.1) from pathogenic Candida glabrata (CgNce103) by 1H-indole-2,3-dione 3-[N-(4-sulfamoylphenyl)thiosemicarbazones] 4a–m was investigated. All the compounds were found to be potent inhibitors of CgNce103, with inhibition constants in the range of 6.4- 63.9 nM. The 5,7-dichloro substituted derivative 4l showed the most effective inhibition (KI of 6.4 nM) as well as the highest selectivity for inhibiting CgNce103 over the cytosolic human (h) isoforms hCA I and II. A possible binding interaction of compound 4l within the active site of CgNce103 has been proposed based on docking studies.eninfo:eu-repo/semantics/openAccessArticleWOS:0004579608000018506110613810.1080/14756366.2018.156404530724625