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Dejstvo tigeciklina na vezivanje fluorohinolona za humani serumski albumin

dc.creatorJelić, Ratomir
dc.creatorStojanović, Stefan D.
dc.creatorBerić, Jelena D.
dc.creatorOdović, Jadranka
dc.date.accessioned2019-09-02T12:03:05Z
dc.date.available2019-09-02T12:03:05Z
dc.date.issued2018
dc.identifier.issn1820-8665
dc.identifier.urihttp://farfar.pharmacy.bg.ac.rs/handle/123456789/3031
dc.description.abstractThe co-administration of several drugs in multidrug therapy may alter the binding of each drug to human serum albumin (HSA) and, thus, their pharmacology effect. Therefore, in this study, the interaction mechanism between HSA and two fluoroquinolones (FQs), sparfloxacin (SPF) and levofloxacin (LVF), was investigated using fluorescence and absorption methods in the absence and presence of the competing drugtigecycline (TGC). The UV-Vis and fluorescence spectroscopy results showed that the fluorescence quenching of HSA was a result of the formation of the HSA-SPF and HSA-LVF complexes. The fluorescence quenching of HSA-TGC revealed that tigecycline can regulate the binding sites, binding mode and binding affinity of fl uoroquinolones. The binding constants (KA) and binding sites (n) of the interaction systems were calculated. The results confirmed that the KA values of the HSA-FQ system decreased in the presence of TGC, indicating that TGC can affect the binding ability of FQ for HSA. This interaction may increase the free plasma concentration of unbound FQ and enhance their pharmacology effect.en
dc.description.abstractIstovremena primena nekoliko lekova, u multilek terapiji, može izmeniti njihovo vezivanje za humani serumski albumin (HSA) i njihov farmakološki efekat. Zbog toga, u ovom radu je proučavan mehanizam interakcije između HSA i dva fluorohinolona (FQs): sparfloksacina (SPF) i levofloksacina (LVF) fluorescentnim i apsorpcionim metodama u odsustvu i prisustvu konkurentskog leka - tigeciklina (TGC). Rezultati UV-Vis i fluorescentne spektroskopije su pokazali da je gašenje fluorescencije u HSA rezultat formiranja HSA-SPF i HSA-LVF kompleksa. Gašenje fluoroscencije u HSA-TGC je pokazalo da tigeciklin može regulisati mesta vezivanja, način vezivanja i afinitet vezivanja fluorohinolona. Konstante vezivanja (KA) i broj vezujućih mesta (n) za interakcije u sistemu su izračunate. Rezultati su potvrdili da su vrednosti KA u HSA-FQ sistemu, smanjene u prisustvu TGC, a to ukazuje da TGC može da utiče na sposobnost vezivanja FQ za HSA. Ova interakcija može povećati slobodnu koncentraciju u plazmi nevezanog FQ i poboljšati njegov farmakološki efekat.sr
dc.publisherUniverzitet u Kragujevcu - Fakultet medicinskih nauka, Kragujevac
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172016/RS//
dc.rightsopenAccess
dc.sourceSerbian Journal of Experimental and Clinical Research
dc.subjectfluorescencijaen
dc.subjecthumani serumski albuminen
dc.subjectfluorohinolonien
dc.subjecttigeciklinen
dc.subjectfluorescencijasr
dc.subjecthumani serumski albuminsr
dc.subjectfluorohinolonisr
dc.subjecttigeciklinsr
dc.titleThe effect of tigecycline on the binding of fluoroquinolones to human serum albuminen
dc.titleDejstvo tigeciklina na vezivanje fluorohinolona za humani serumski albuminsr
dc.typearticle
dc.rights.licenseARR
dcterms.abstractСтојановић, Стефан Д.; Јелић, Ратомир; Одовић, Јадранка; Берић, Јелена Д.; Дејство тигециклина на везивање флуорохинолона за хумани серумски албумин; Дејство тигециклина на везивање флуорохинолона за хумани серумски албумин;
dc.citation.volume19
dc.citation.issue1
dc.citation.spage17
dc.citation.epage25
dc.citation.other19(1): 17-25
dc.citation.rankM51
dc.identifier.doi10.1515/SJECR-2017-0006
dc.identifier.scopus2-s2.0-85044772700
dc.identifier.fulltexthttp://farfar.pharmacy.bg.ac.rs//bitstream/id/1638/3029.pdf
dc.identifier.rcubconv_1040
dc.type.versionpublishedVersion


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