SAR and molecular mechanism studies of monoamine oxidase inhibition by selected chalcone analogs.

ABSTRACT: The present study describes the synthesis of a series of 22 chalcone analogs. These compounds were evaluated as potential human MAO-A and MAO-B inhibitors. The compounds showed varied selectivity against the two isoforms. The IC₅₀ values were found to be in the micromolar to submicromolar range. The K_i values of compound 16 were determined to be 0.047 and 0.020 μM for the inhibition of MAO-A and MAO-B, respectively. Dialysis of enzyme-inhibitor mixtures indicated a reversible competitive mode of inhibition. Most of the synthesized chalcone analogs showed a better selectivity toward MAO-B. However, introducing of 2,4,6-trimethoxy substituents on ring B shifted the selectivity toward MAO-A. In addition, we investigated the molecular mechanism of MAO-B inhibition by sele

SUBMITTER: Shalaby R 

PROVIDER: S-EPMC6442233 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature