Synthesis, characterization of some new hydrazone derivatives and investigation of their carbonic anhydrase and cholinesterse enzyme inhibation activities

Human carbonic anhydrase I and II isoenzymes (hCA I and II) and cholinesterase enzymes, namely acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) are important metabolic enzymes closely associated with various physiological and pathological processes. In this study, we investigated the inhibitory action of some novel hybrid molecules containing hydrazone and sulfonate moieties, namely novel hydrazone derivatives (2a-g) based on aryl sulfonate compounds (1a-g), against selected metabolic enzymes including hCA I, hCA II, AChE and BChE. The chemical structures of hybrids were characterized by elemental analysis and some spectroscopic techniques. All tested hybrid compounds showed low nanomolar inhibition with IC50 values of in the range of 30.4 to 264.0 nM against hCA I, 23.2 to 251.6 nM against hCA II, 12.1 to 114.3 nM against AChE, and 76.4 to 134.0 nM against BChE. These compounds inhibited hCA I and AChE more than reference molecules acetazolamide (AZA) and neostigmine. Among the tested compounds, compounds 2c and 2e were determined to be the best inhibitors against these enzymes.