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dc.contributor.authorBerk, Barkın
dc.contributor.authorKaynar, Gürmen
dc.contributor.authorErtaş, Merve
dc.contributor.authorBiltekin, Sevda Nur
dc.date.accessioned10.07.201910:49:13
dc.date.accessioned2019-07-10T19:36:14Z
dc.date.available10.07.201910:49:14
dc.date.available2019-07-10T19:36:14Z
dc.date.issued2017en_US
dc.identifier.citationBerk, B., Kaynar, G., Ertaş, M. ve Biltekin, S.N. (2017). Molecular modelling and compound activity of the escherichia coli and staphylococcus aureus DNA gyrase B ATPase site. Acta Pharmaceutica Sciencia, 55(1), 97-117. https://dx.doi.org/10.23893/1307-2080.APS.0557en_US
dc.identifier.issn1307-2080
dc.identifier.urihttps://hdl.handle.net/20.500.12511/1105
dc.identifier.urihttps://dx.doi.org/10.23893/1307-2080.APS.0557
dc.description.abstractDevelopment of new treatment ligands that can distinguish Escherichia coli (E. coli) from Staphylococcus aureus (S. aureus) is important because of bacterium multiple drug resistance. High-throughput virtual screening (HTVS), docking-scoring and receiver operating characteristic curves are essential components of computational methods used in designing potential new ligands. Here, we investigated the E. coli and S. aureus DNA gyrase B active site; amino acid, water molecule, and ligand interactions using crystallographic data and HTVS to determine potential hits. Trial and test sets were prepared from the 5000 and 50000 compounds of the ZINC databases with known E. coli and S. aureus DNA gyrase B ATPase inhibitor molecules. Trial sets were evaluated and screened by determining the contribution of water molecules to interactions. Data analysis led to the identification of novel interaction patterns, which were screened over a test set; 20 maximum scored compounds were identified and further tested against the novobiocin standard with gel-based E. coli and S. aureus supercoiling assays. The highest scoring N’-(1-naphthylcarbonyl)-2, 1, 3-benzothi-adiazole-5-carbohydrazide structure showed selective inhibition with E. coli and S. aureus DNA gyrase B ATPases. We determined that in terms of selectivity, some water molecules have a major impact on amino acid-ligand interactions.en_US
dc.language.isoengen_US
dc.publisherUniversity of Istanbulen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectDNA Gyrase B ATPaseen_US
dc.subjectDockingen_US
dc.subjectEscherichia Colien_US
dc.subjectHTVSen_US
dc.subjectROC Curvesen_US
dc.subjectStaphylococcus Aureusen_US
dc.titleMolecular modelling and compound activity of the escherichia coli and staphylococcus aureus DNA gyrase B ATPase siteen_US
dc.typearticleen_US
dc.relation.ispartofActa Pharmaceutica Scienciaen_US
dc.departmentİstanbul Medipol Üniversitesi, Eczacılık Fakültesi, Eczacılık Meslek Bilimleri Bölümü, Farmasötik Kimya Ana Bilim Dalıen_US
dc.authorid0000-0001-6047-2796en_US
dc.authorid0000-0002-2289-7950en_US
dc.authorid0000-0003-1896-2729en_US
dc.identifier.volume55en_US
dc.identifier.issue1en_US
dc.identifier.startpage97en_US
dc.identifier.endpage117en_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.identifier.doi10.23893/1307-2080.APS.0557en_US
dc.identifier.scopusqualityQ4en_US


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