N-Acylsulfonamides strongly inhibit human carbonic anhydrase isoenzymes I and II

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Yıldırım A., Atmaca U., Keskın A., Topal M., Çelik M., Gülçin İ., ...Daha Fazla

BIOORGANIC & MEDICINAL CHEMISTRY, cilt.23, sa.10, ss.2598-2605, 2015 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 23 Sayı: 10
  • Basım Tarihi: 2015
  • Doi Numarası: 10.1016/j.bmc.2014.12.054
  • Dergi Adı: BIOORGANIC & MEDICINAL CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.2598-2605
  • Anahtar Kelimeler: Sulfonamide, Imide, N-Acylsulfonamide, Carbonic anhydrase, Enzyme purification, Enzyme inhibition, TROUT ONCORHYNCHUS-MYKISS, ERYTHROCYTE ISOZYMES I, ISOFORMS I, SULFONAMIDE DERIVATIVES, ENZYME-ACTIVITY, CDNA CLONING, BOVINE-MILK, VITRO, PURIFICATION, LACTOPEROXIDASE
  • Atatürk Üniversitesi Adresli: Evet

Özet

Sulfonamides represent a significant class of biologically active compounds that inhibit carbonic anhydrase (CA, EC.: 4.2.1.1) isoenzymes involved in different pathological and physiological events. Sulfonamide CA inhibitors are used therapeutically as diuretic, antiglaucoma, antiobesity and anticancer agents. A series of new sulfonamides were synthesized using imides and tosyl chloride as starting materials. These N-acylsulfonamides efficiently inhibited the cytosolic human carbonic anhydrase isoenzymes I, and II (hCA I, and II), with nanomolar range inhibition constants ranging between 36.4 +/- 6.0-254.6 +/- 18.0 and 58.3 +/- 0.6-273.3 +/- 2.5 nM, respectively. (C) 2015 Elsevier Ltd. All rights reserved.