Synthesis and carbonic anhydrase inhibitory properties of novel coumarin derivatives

Karataş M. O., Alıcı B., Çakır Ü., Cetinkaya E., Demir D., Ergün A., ...Daha Fazla

JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, cilt.28, sa.2, ss.299-304, 2013 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 28 Sayı: 2
  • Basım Tarihi: 2013
  • Doi Numarası: 10.3109/14756366.2012.677838
  • Dergi Adı: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED)
  • Sayfa Sayıları: ss.299-304
  • Anahtar Kelimeler: Carbonic anhydrase, coumarin, benzimidazolium, inhibition, IN-VITRO INHIBITION, HETEROCYCLIC SULFONAMIDES, AROMATIC/HETEROCYCLIC SULFONAMIDES, SULFAMATE INHIBITORS, HUMAN SERUM, PURIFICATION, TARGET, PARAOXONASE, PESTICIDES, ACTIVATORS
  • İnönü Üniversitesi Adresli: Evet

Özet

A newly series of water-soluble 1-alkyl-3-(4-methyl-7, 8-dihydroxy-2H-chromen-2-one) benzimidazolium chloride salts (3a-j) were synthesized and their inhibitory effects on the activity of purified human carbonic anhydrase (hCA) I and II were evaluated. hCA I and II from human erythrocytes were purified by a simple one step procedure by using Sepharose 4B-L-tyrosine-sulphanilamide affinity column. The result showed that all the synthesized compounds were inhibited the CA isoenzymes activity. Among them, 3g and 3j were found to be most active (IC50 = 22.09 mu M and 20.33 mu M) for hCA I and hCA II, respectively.