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dc.creatorMarković, Olivera
dc.creatorCvijetić, Ilija
dc.creatorZlatović, Mario
dc.creatorOpsenica, Igor
dc.creatorKonstantinović, Jelena M.
dc.creatorTerzić-Jovanović, Nataša
dc.creatorŠolaja, Bogdan
dc.creatorVerbić, Tatjana
dc.date.accessioned2019-01-30T18:01:13Z
dc.date.available2019-01-30T18:01:13Z
dc.date.issued2018
dc.identifier.issn1386-1425
dc.identifier.urihttp://cer.ihtm.bg.ac.rs/handle/123456789/2472
dc.description.abstractInteractions between eight in-house synthesized aminoquinolines, along with well-known chloroquine, and human serum albumin (HSA) have been studied by fluorescence spectroscopy. The synthesized aminoquinolines, despite being structurally diverse, were found to be very potent antimalarials. Fluorescence measurements indicate that three compounds having additional thiophene or benzothiophene substructure bind more strongly to HSA than other studied compounds. Competitive binding experiments indicate that these three compounds bind significantly stronger to warfarin compared to diazepam binding site. Fluorescence quenching at three temperatures (20, 25, and 37 degrees C) was analyzed using classical Stern-Volmer equation, and a static quenching mechanism was proposed. The enthalpy and entropy changes upon sulphur-containing compound-HSA interactions were calculated using Van't Hoff equation. Positive values of enthalpy and entropy changes indicate that non-specific, hydrophobic interactions are the main contributors to HSA-compound interaction. Molecular docking and calculated lipophilicity descriptors indicate the same, pointing out that the increased lipophilicity of sulphur-containing compounds might be a reason for their better binding to HSA. Obtained results might contribute to design of novel derivatives with improved-pharmacokinetic properties and drug efficacy.en
dc.publisherPergamon-Elsevier Science Ltd, Oxford
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172008/RS//
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172035/RS//
dc.relationinfo:eu-repo/grantAgreement/EC/FP7/256716/EU//
dc.relationSerbian Academy of Sciences and Arts [F80]
dc.rightsrestrictedAccess
dc.sourceSpectrochimica Acta Part A-Molecular and Biomolecular Spectroscopy
dc.subjectAminoquinolinesen
dc.subjectHuman serum albuminen
dc.subjectFluorescence spectroscopyen
dc.subjectBinding affinityen
dc.subjectMolecular dockingen
dc.subjectStem-Volmer ploten
dc.titleHuman serum albumin binding of certain antimalarialsen
dc.typearticle
dc.rights.licenseARR
dcterms.abstractМарковић, Оливера; Златовиц, Марио В.; Константиновиц, Јелена М.; Солаја, Богдан A.; Опсеница, Игор М.; Цвијетић, Илија Н.; Терзић Јовановић, Наташа; Вербиц, Татјана З.;
dc.citation.volume192
dc.citation.spage128
dc.citation.epage139
dc.citation.other192: 128-139
dc.citation.rankM21
dc.identifier.pmid29128746
dc.identifier.doi10.1016/j.saa.2017.10.061
dc.identifier.rcubConv_3871
dc.identifier.scopus2-s2.0-85032915981
dc.identifier.wos000424716900019
dc.type.versionpublishedVersion


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