JOURNAL OF HETEROCYCLIC CHEMISTRY, vol.57, no.5, pp.2225-2233, 2020 (SCI-Expanded)
Monoamine oxidases (MAO) are enzymes that catalyze the oxidative deamination of monoamines such as dopamine, noradrenaline, adrenaline, and serotonin. Recent studies have shown that numerous benzothiazole derivatives exhibit hMAO inhibitory activity in the micromolar concentration range. In this study, a novel series of benzothiazole-thiadiazole (5a-5l) was synthesized and characterized their chemical structures by H-1-NMR, C-13-NMR, and Mass spectroscopy. These compounds were evaluated as inhibitors for types A and B MAO enzymes. Compounds 5f and 5l were the most active derivatives in the series with an IC50 values of 0.107 +/- 0.003 and 0.128 +/- 0.004, respectively. Furthermore, cytotoxicity of compounds 5f and 5l were investigated and found as non-cytotoxic.