Yelekçi, KemalToprakçı, MustafaYelekçi, Kemal2019-06-272019-06-272005560960-894X1464-34050960-894X1464-3405https://hdl.handle.net/20.500.12469/117https://doi.org/10.1016/j.bmcl.2005.07.043Monoamine oxidase (EC1.4.3.4MAO) is a mitochondrial outer membrane flavoenzyme that catalyzes the oxidation of biogenic 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 targets for antidepressant and neuroprotective drugs. Elucidation of the X-ray crystallographic structure of MAO-B has opened the way for molecular modeling studies. A series of experimentally tested (1-10) model compounds has been docked computationally to the active site of the MAO-B enzyme. The AutoDock 3.0.5 program was employed to perform automated molecular docking. The free energies of binding (Delta G) and inhibition constants (K-i) of the docked compounds were calculated by the Lamarckian Genetic Algorithm (LGA) of AutoDock 3.0.5. Excellent to good correlations between the calculated and experimental K-i values were obtained. (c) 2005 Elsevier Ltd. All rights reserved.eninfo:eu-repo/semantics/openAccessDockingMAO-B inhibitorsArticle443844462015WOS:00023193670000610.1016/j.bmcl.2005.07.0432-s2.0-24344445524N/AQ216137882