Paper Title
Synthesis and Biological Activity Evaluation of New Thiazolylhydrazine Derivatives

Monoamine oxidases (MAO) are enzymes that catalyze the oxidative deamination of monoamines such as dopamine, noradrenaline, adrenaline and serotonin. MAOs are located in the mitochondrial outer membrane of neuronal, glial and other cells. This enzyme consists of two isoforms, MAO-A and MAO-B. While MAO-A selective inhibitors became important in the treatment of depression, MAO-B inhibitors were introduced as promising drugs in the treatment of parkinson's. Recent studies have shown that numerous thiazolylhydrazine derivatives exhibit hMAO inhibitory activity in the micromolar concentration range. Thus, in this study six new thiazolylhydrazine-piperazine derivatives were designed and synthesized to able to have good inhibition profile as cholinesterase inhibitors. The structures of synthesized compounds were confirmed via 1H and 13C NMR spectroscopic methods. The monoamineoxidase inhibitor activity of final compounds was performed. According to enzyme inhibition assay, none of the compounds displayed significant inhibitory activity against MAO-B enzyme. On the other hand, compound 2b showed promising inhibition potency against MAO-A enzyme with IC50 values of 0.198±0.009 µM. Keywords - Monoamine Oxidase Inhibitors, Enzyme Activity, Thiazolylhydrazine, Piperazine