Synthesis and Carbonic Anhydrase Inhibitory Effects of Novel Sulfamides Derived from 1-Aminoindanes and Anilines
ARCHIV DER PHARMAZIE, cilt.347, sa.12, ss.950-957, 2014 (SCI-Expanded, Scopus)
- Yayın Türü: Makale / Tam Makale
- Cilt numarası: 347 Sayı: 12
- Basım Tarihi: 2014
- Doi Numarası: 10.1002/ardp.201400257
- Dergi Adı: ARCHIV DER PHARMAZIE
- Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
- Sayfa Sayıları: ss.950-957
- Anahtar Kelimeler: Aminoindane, Aniline, Carbonic anhydrase, Enzyme inhibition, Sulfamide, Sulfamoyl carbamate, TROUT ONCORHYNCHUS-MYKISS, ERYTHROCYTES IN-VITRO, ISOZYMES I, SULFONAMIDE DERIVATIVES, ENZYME-ACTIVITY, ANTIOXIDANT, SERIES, PURIFICATION, DANTROLENE, MUTATIONS
- Atatürk Üniversitesi Adresli: Evet
Özet
Three 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 one-step 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 the most potent inhibitory effect against hCA I (K-i: 153.88 nM), while sulfamide derivative 26 showed the highest inhibitory potential against hCA II (K-i: 117.80 nM).