Carbonic anhydrase and acetylcholinesterase inhibitory effects of carbamates and sulfamoylcarbamates

Gocer H., Akincioglu A., GÖKSU S., GÜLÇİN İ., Supuran C. T.

JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, cilt.30, sa.2, ss.316-320, 2015 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 30 Sayı: 2
  • Basım Tarihi: 2015
  • Doi Numarası: 10.3109/14756366.2014.928704
  • Dergi Adı: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.316-320
  • Anahtar Kelimeler: Acetylcholinesterase, AChE, CA, carbamates, carbonic anhydrase, enzyme inhibition, TROUT ONCORHYNCHUS-MYKISS, ERYTHROCYTES IN-VITRO, ISOFORMS I, SULFONAMIDE DERIVATIVES, LIPID-PEROXIDATION, ENZYME-ACTIVITIES, ISOZYMES I, ANTIOXIDANT, MELATONIN, PURIFICATION
  • Atatürk Üniversitesi Adresli: Evet

Özet

Carbonic anhydrases (CA), as a family of metalloenzymes, are found in almost every type of tissue and play an important role in catalyzing the equilibration of carbon dioxide and carbonic acid. In this study, a series of carbamate derivative was synthesized, and their inhibition effects on hCA I, hCA II and acetylcholinesterase (AChE) enzymes were investigated. They were determined to be very good inhibitor against for both isoenzymes (hCA I and hCA II) and AChE. The hCA I and hCA II were effectively inhibited by the carbamate derivatives, with inhibition constants (K-i) in the range of 194.4-893.5nM (for hCA I) and 103.9-835.7 nM (for hCA II). On the other hand, K-i parameters of these compounds for AChE enzyme inhibition were determined in the range of 12.0-61.3 nM. The results clearly showed that both CA isoenzymes and AChE were inhibited by carbamate derivatives at the nM levels.