The human carbonic anhydrase isoenzymes I and II (hCA I and II) inhibition effects of trimethoxyindane derivatives

TASLIMI P., GÜLÇİN İ., ÖZGERIŞ B., GÖKSU S., Tumer F., ALWASEL S. H., ...Daha Fazla

JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, cilt.31, sa.1, ss.152-157, 2016 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 31 Sayı: 1
  • Basım Tarihi: 2016
  • Doi Numarası: 10.3109/14756366.2015.1014476
  • Dergi Adı: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.152-157
  • Anahtar Kelimeler: Acetylcholine esterase, affinity chromatography carbonic anhydrase, enzyme inhibition, enzyme purification, trimethoxyindane derivatives, TROUT ONCORHYNCHUS-MYKISS, ISOFORMS I, SULFONAMIDE DERIVATIVES, ACETYLCHOLINE ESTERASE, ENZYME-ACTIVITY, BOVINE-MILK, ISOZYMES I, VITRO, LACTOPEROXIDASE, PURIFICATION
  • Atatürk Üniversitesi Adresli: Evet

Özet

Carbonic anhydrases (CAs, EC 4.2.1.1) had six genetically distinct families described to date in various organisms. There are 16 known CA isoforms in humans. Human CA isoenzymes I and II (hCA I and hCA II) are ubiquitous cytosolic isoforms. Acetylcholine esterase (AChE. EC 3.1.1.7) is a hydrolase that hydrolyzes the neurotransmitter acetylcholine relaying the signal from the nerve. In this study, some trimethoxyindane derivatives were investigated as inhibitors against the cytosolic hCA I and II isoenzymes, and AChE enzyme. Both hCA isozymes were inhibited by trimethoxyindane derivatives in the low nanomolar range. These compounds were good hCA I inhibitors (Kis in the range of 1.66-4.14nM) and hCA II inhibitors (Kis of 1.37-3.12nM) and perfect AChE inhibitors (Kis in the range of 1.87-7.53nM) compared to acetazolamide as CA inhibitor (Ki: 6.76nM for hCA I and Ki: 5.85nM for hCA II) and Tacrine as AChE inhibitor (Ki: 7.64nM).