Synthesis, enzyme activity and molecular docking studies of new benzylamine-sulfonamide derivatives as selective MAO-B inhibitors.

Many studies have been conducted on the selective inhibition of human monoamine oxidase B (MAO-B) enzyme using benzylamine-sulphonamide derivatives. Using various chemical modifications on , which was reported previously by our team and showed a significant level of MAO-B inhibition, novel benzylamine-sulphonamide derivatives were designed, synthesised, and their MAO inhibition potentials were evaluated. Among the tested derivatives, compounds and achieved IC values of 0.041 ± 0.001 µM and 0.065 ± 0.002 µM, respectively. The mechanism of MAO-B inhibition by compounds and was studied using Lineweaver-Burk plot. The nature of inhibition was also determined to be non-competitive. Cytotoxicity tests were conducted and compounds and were found to be non-toxic. Molecular docking studies were also carried out for compound , which was found as the most potent agent, within MAO-B catalytic site.