2026-10-23T14:55:13Zhttps://gumushane-rdlopen.rawdatalibrary.net/oai/requestoai:gumushane-rdlopen.rawdatalibrary.net:gumushane/155232026-10-22T11:37:59Zopenairecom_gumushane_10000col_gumushane_10001com_gumushane_10010col_gumushane_10182Synthesis and carbonic anhydrase inhibitory effects of novel sulfamides derived from 1-aminoindanes and anilinesAkbaba, YusufBastem, EnesTopal, FevziGülçin, IlhamiMarasç, AhmetGöksu, SüleymanAminoindane /Aniline /Carbonic anhydrase /Enzyme inhibition /Sulfamide /Sulfamoyl carbamateThree 1-aminoindanes, four anilines and BnOH or t-BuOH were reacted with chlorosulfonyl isocyanate to give sulfamoyl carbamates. Pd-C catalysed hydrogenolysis reactions of carbamates or deprotection of the Boc group of the carbamates with CF3CO2H afforded seven novel sulfamides. Human carbonic anhydrase (hCA) isoenzymes I and II (hCA I and hCA II) were purified from fresh human blood erythrocytes with onestep affinity chromatography on Sepharose 4B-tyrosine-sulfanilamide. The inhibitory properties of the novel sulfamides on both isoenzymes were determined using the esterase activity with 4-nitrophenyl acetate (NPA) as substrate. The tested novel sulfamides derived from 1-aminoindanes and anilines effectively inhibited hCA I and II competitively in the nanomolar range. Among these compounds, the novel sulfamide derivative 17 showed themost potent inhibitory effect against hCA I (Ki: 153.88 nM), while sulfamide derivative 26 showed the highest inhibitory potential against hCA II (Ki: 117.80nM).Wiley-VCH Verlag2014Articlehttps://rdlopen.rawdatalibrary.net/r/gumushane/15523https://doi.org/10.1002/ardp.2014002570365-6233enArchiv der Pharmazieinfo:eu-repo/semantics/closedAccessinfo:eu-repo/semantics/articlehttps://gumushane-rdlopen.rawdatalibrary.net/tr/items/gumushane/15523