Functionalized imidazolium and benzimidazolium salts as paraoxonase 1 inhibitors: Synthesis, characterization and molecular docking studies

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dc.authoridKarataş, Mert Olgun/0000-0001-8500-2088
dc.authoridGençer, Nahit/0000-0001-7092-8857
dc.authoridARSLAN, N Burcu/0000-0002-1880-1047
dc.authoridÖzdemir, Namık/0000-0003-3371-9874
dc.authoridUSLU, HARUN/0000-0001-8827-8557
dc.authoridGençer, Nahit/0000-0001-7092-8857
dc.authoridALICI, Bulent/0000-0001-5009-3223
dc.authorwosidKarataş, Mert Olgun/ABG-7848-2020
dc.authorwosidGençer, Nahit/HHD-1544-2022
dc.authorwosidARSLAN, N Burcu/A-3634-2019
dc.authorwosidÖzdemir, Namık/J-6434-2015
dc.authorwosidUSLU, HARUN/P-3681-2019
dc.authorwosidGençer, Nahit/AAG-4507-2019
dc.authorwosidArslan, Nahide/KHE-4361-2024
dc.contributor.authorKaratas, Mert Olgun
dc.contributor.authorUslu, Harun
dc.contributor.authorAlici, Bulent
dc.contributor.authorGokce, Basak
dc.contributor.authorGencer, Nahit
dc.contributor.authorArslan, Oktay
dc.contributor.authorArslan, N. Burcu
dc.date.accessioned2024-08-04T20:41:32Z
dc.date.available2024-08-04T20:41:32Z
dc.date.issued2016
dc.departmentİnönü Üniversitesien_US
dc.description.abstractParaoxonase (PON) is a key enzyme in metabolism of living organisms and decreased activity of PON1 was acknowledged as a risk for atherosclerosis and organophosphate toxicity. The present study describes the synthesis, characterization, PON1 inhibitory properties and molecular docking studies of functionalized imidazolium and benzimidazolium salts (1a-5g). The structures of all compounds were elucidated by IR, NMR, elemental analysis and structures of compounds 2b and 2c were characterized by single-crystal X-ray diffraction. Compound 1c, a coumarin substituted imidazolium salt showed the best inhibitory effect on the activity of PON1 with good IC50 value (6.37 mu M). Kinetic investigation was evaluated for this compound and results showed that this compound is competitive inhibitor of PON1 with K-1, value of 2.39 mu M. Molecular docking studies were also performed for most active compound 1c and one of least active compound 2c in order to determine the probable binding model into active site of PON1 and validation of the experimental results. (C) 2016 Elsevier Ltd. All rights reserved.en_US
dc.identifier.doi10.1016/j.bmc.2016.02.012
dc.identifier.endpage1401en_US
dc.identifier.issn0968-0896
dc.identifier.issn1464-3391
dc.identifier.issue6en_US
dc.identifier.pmid26879855en_US
dc.identifier.scopus2-s2.0-84958926372en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage1392en_US
dc.identifier.urihttps://doi.org/10.1016/j.bmc.2016.02.012
dc.identifier.urihttps://hdl.handle.net/11616/97185
dc.identifier.volume24en_US
dc.identifier.wosWOS:000370822700026en_US
dc.identifier.wosqualityQ2en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.publisherPergamon-Elsevier Science Ltden_US
dc.relation.ispartofBioorganic & Medicinal Chemistryen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectBenzimidazoliumen_US
dc.subjectCoumarinen_US
dc.subjectImidazoliumen_US
dc.subjectInhibitionen_US
dc.subjectMolecular dockingen_US
dc.subjectParaoxonase 1en_US
dc.titleFunctionalized imidazolium and benzimidazolium salts as paraoxonase 1 inhibitors: Synthesis, characterization and molecular docking studiesen_US
dc.typeArticleen_US

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