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

Abstract

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 1.66–4.14 nM) and hCA II inhibitors (Kis of 1.37–3.12 nM) and perfect AChE inhibitors (Kis in the range of 1.87–7.53 nM) compared to acetazolamide as CA inhibitor (Ki: 6.76 nM for hCA I and Ki: 5.85 nM for hCA II) and Tacrine as AChE inhibitor (Ki: 7.64 nM).

• Acetylcholine esterase
• affinity chromatography carbonic anhydrase
• enzyme inhibition
• enzyme purification
• trimethoxyindane derivatives

Declaration of interest

The authors declare no conflict of interest. IG and SHE would like to extend their sincere appreciation to the Deanship of Research Chairs Program at King Saud University for funding this research, RGP-VPP-254.