Inhibition of human carbonic anhydrase isozymes I, II and VI with a series of bisphenol, methoxy and bromophenol compounds

Balaydin H. T., Durdagi S., Ekinci D., Senturk M., GÖKSU S., MENZEK A.

JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, cilt.27, sa.4, ss.467-475, 2012 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 27 Sayı: 4
  • Basım Tarihi: 2012
  • Doi Numarası: 10.3109/14756366.2011.596836
  • Dergi Adı: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.467-475
  • Anahtar Kelimeler: Carbonic anhydrase, molecular docking, bisphenol, bromophenol, hCA II, hCA VI, ERYTHROCYTE GLUTATHIONE-REDUCTASE, THERAPEUTIC APPLICATIONS, VITRO INHIBITION, METAL-COMPLEXES, SULFONAMIDES, PURIFICATION, THIOXOLONE, DRUGS
  • Recep Tayyip Erdoğan Üniversitesi Adresli: Hayır

Özet

Carbonic anhydrase inhibitors (CAI) are valuable molecules as they have several therapeutic applications, including anti-glaucoma activity. In this study, inhibition of three human carbonic anhydrase (hCA, EC 4.2.1.1) isozymes I, II and VI with a series of bisphenol and bromophenol derivatives was investigated. Molecular docking studies of a set of such inhibitors within CA I and II were also performed. K-I values of the molecules 2-9 were in the range of 10.025-892.109 mu M for hCA I, 1.437-59.107 mu M for hCA II and 11.143-919.182 mu M for hCA VI, respectively. Reported inhibitory activities of molecules 2-9 will assist in better understanding of structure-activity relationship studies of CAI.