Abstract
Abstract A series of substituted (Z)-3-benzylideneisobenzofuran-1(3H)-ones have been designed, synthesized, and biologically evaluated in vitro on human monoamine oxidase A/B (hMAO-A/B). Some compounds were potent to inhibit hMAO-B isoenzyme. Especially compound 20 showed an IC50 value of 8.4 nM and a selectivity index more than 1000 folds. Docking experiments and molecular dynamic simulation results showed that this series might bind to the active pocket in the catalytic center and stabilize the protein. This work provided a new type of skeleton for MAO-B inhibitor design, which might benefit the development of Parkinson's disease medicine.
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