Synthesis and Carbonic Anhydrase Inhibitory Effects of Novel Sulfamides Derived from 1-Aminoindanes and Anilines

Akbaba Y., BASTEM E., TOPAL F., GÜLÇİN İ., MARAŞ A., GÖKSU S.

ARCHIV DER PHARMAZIE, cilt.347, sa.12, ss.950-957, 2014 (SCI-Expanded) identifier identifier identifier

  • 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).