In silico prediction of logP, total polar surface area (TPSA), and drug likeness (Lipinski Rule of 5) were determined using the SwissADME server [33 (link)]. Docking studies were performed using MOE 2019 (Chemical Computing Group). The protein structure referenced for MAO-B was 2v5z.pdb and for AChE 4ey7.pdb. In the MAO-B enzyme file two chains are crystalized and chain B was deleted before docking was carried out. Protein was prepared before docking by protonation of amino acids at pH 7.4. The binding site was identified as the area where co-crystallized ligand was located. Since MOE recognizes FAD as a part of the ligand set, we first designated the true ligand as so that MOE could use it in the docking run. Only the top-returned binding pose (most negative binding energy) of each ligand was further evaluated. The induced-fit binding mode was used to study the ligand-protein interaction, and solvent was allowed part of the docking calculation. As control docking experiment, the root-square mean deviation (RMSD) was calculated for each of the two enzymes. A RSMD < 2 Å was considered adeqote for our studies [34 (link)].