Yelekci, K.Karahan, O.Toprakci, M.2024-10-152024-10-152007190300-95641435-1463https://doi.org/10.1007/s00702-007-0679-7https://hdl.handle.net/20.500.12469/6322Karahan, Ozlem/0000-0003-4916-9715; Yelekci, Kemal/0000-0002-0052-4926Monoamine oxidase (MAO, EC 1.4.3.4) is a flavoenzyme bound to the mitochondrial outer membranes of the cells, which is responsible for the oxidative deamination of neurotransmitter and dietary amines. It has two distinct isozymic forms, designated MAO-A and MAO-B, each displaying different substrate and inhibitor specificities. They are the well-known target for antidepressant, Parkinson's disease and neuroprotective drugs. Elucidation of the x-ray crystallographic structure of MAO-B has opened the way for molecular modeling studies. In this research 12 reversible and MAO-B selective inhibitors have been docked computationally to the active site of the MAO-B enzyme. AutoDock 3.0.5 was employed to perform the automated molecular docking. The result of docking studies generated thermodynamic properties, such as free energy of bindings (Delta G(b)) and inhibition constants (K-i) for the inhibitors. Moreover, 3D pictures of inhibitor-enzyme complexes afforded valuable data regarding the binding orientation of each inhibitor in the active site of MAO-B.eninfo:eu-repo/semantics/closedAccessdocking calculationsreversible MAO-B inhibitorsthree dimentional picture of inhibitor-enzyme complexConference Object7257326114WOS:00024673510000910.1007/s00702-007-0679-72-s2.0-34250792398Q217401533