The human carbonic anhydrase isoenzymes I and II (hCA I and II) inhibition effects of trimethoxyindane derivatives
JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, cilt.31, sa.1, ss.152-157, 2016 (SCI-Expanded, Scopus)
- 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).