Docking of Novel Reversible Monoamine Oxidase-B Inhibitors

dc.authorid Karahan, Ozlem/0000-0003-4916-9715
dc.authorid Yelekci, Kemal/0000-0002-0052-4926
dc.authorscopusid 6506158277
dc.authorscopusid 56483354100
dc.authorscopusid 6506900925
dc.authorwosid Karahan, Ozlem/O-3156-2019
dc.authorwosid Yelekci, Kemal/B-1431-2019
dc.contributor.author Yelekci, K.
dc.contributor.author Karahan, O.
dc.contributor.author Toprakci, M.
dc.date.accessioned 2024-10-15T19:39:29Z
dc.date.available 2024-10-15T19:39:29Z
dc.date.issued 2007
dc.department Kadir Has University en_US
dc.department-temp Kadir Has Univ, Fac Arts & Sci, TR-34231 Istanbul, Turkey; Bogazici Univ, Fac Arts & Sci, Dept Chem, Istanbul, Turkey; Istanbul Bilim Univ, Dept Biochem, Sch Med, Istanbul, Turkey en_US
dc.description Karahan, Ozlem/0000-0003-4916-9715; Yelekci, Kemal/0000-0002-0052-4926 en_US
dc.description.abstract Monoamine 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. en_US
dc.description.woscitationindex Science Citation Index Expanded - Conference Proceedings Citation Index - Science
dc.identifier.citationcount 19
dc.identifier.doi 10.1007/s00702-007-0679-7
dc.identifier.endpage 732 en_US
dc.identifier.issn 0300-9564
dc.identifier.issn 1435-1463
dc.identifier.issue 6 en_US
dc.identifier.pmid 17401533
dc.identifier.scopus 2-s2.0-34250792398
dc.identifier.scopusquality Q2
dc.identifier.startpage 725 en_US
dc.identifier.uri https://doi.org/10.1007/s00702-007-0679-7
dc.identifier.uri https://hdl.handle.net/20.500.12469/6322
dc.identifier.volume 114 en_US
dc.identifier.wos WOS:000246735100009
dc.language.iso en en_US
dc.publisher Springer Wien en_US
dc.relation.ispartof 12th Amine Oxidase and Trace Amines Workshop (AO 2006) -- JUL 30-AUG 03, 2006 -- Rotterdam, NETHERLANDS en_US
dc.relation.publicationcategory Konferans Öğesi - Uluslararası - Kurum Öğretim Elemanı en_US
dc.rights info:eu-repo/semantics/closedAccess en_US
dc.scopus.citedbyCount 22
dc.subject docking calculations en_US
dc.subject reversible MAO-B inhibitors en_US
dc.subject three dimentional picture of inhibitor-enzyme complex en_US
dc.title Docking of Novel Reversible Monoamine Oxidase-B Inhibitors en_US
dc.type Conference Object en_US
dc.wos.citedbyCount 20
dspace.entity.type Publication

Files