Electrochemical and in silico study of the interaction between phenazopyridine and bovine serum albumin

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dc.authoridalagoz, mehmet abdullah/0000-0001-5190-7196
dc.authoridKuyumcu Savan, Ebru/0000-0002-8851-0907
dc.authoridKAZICI, Dilek/0000-0002-0437-5905
dc.authorwosidalagoz, mehmet abdullah/W-7847-2018
dc.authorwosidKuyumcu Savan, Ebru/E-3430-2019
dc.contributor.authorKazici, Dilek
dc.contributor.authorAlagoez, Mehmet Abdullah
dc.contributor.authorSavan, Ebru Kuyumcu
dc.date.accessioned2024-08-04T20:53:26Z
dc.date.available2024-08-04T20:53:26Z
dc.date.issued2024
dc.departmentİnönü Üniversitesien_US
dc.description.abstractIn this study, an electrochemical sensor was developed using a simple methodology to investigate for the first time the interaction of phenazopyridine with bovine serum albumin (BSA). The modified sensor was fabricated by electropolymerized diphenylamine-4-sulfonic acid barium salt onto the glassy carbon electrode surface by the cyclic voltammetry technique. Very low detection limit and quantification limit values were obtained by differential pulse voltammetry (DPV) in 0.1 M NaClO4 as 0.13 mu M and 0.43 mu M, respectively. In addition, the interference effect was studied, and recovery studies were performed in urine samples achieving dramatic recovery values. Selective and reproducible determinations of phenazopyridine were performed perfectly with the developed sensor. The reduction in BSA oxidation signals as measured by DPV upon incubation with different phenazopyridine concentrations indicated that phenazopyridine was bound to BSA. The currents of the BSA peaks decreased linearly with the phenazopyridine concentration in the linear concentration range (2.00-22.60 mu M). The results of the DPV experiments showed the formation of the BSA-Phenazopyridine complex. Binding parameters such as binding constants and binding free energy were calculated with the voltammetric data. Molecular docking and molecular dynamics simulation studies were performed to learn more about the interaction mechanism between phenazopyridine and BSA. Residues in the active gorge of BSA playing an important role in binding were determined by in silico studies. In silico studies showed that phenazopyridine binds to BSA with high affinity and this binding was stable. Eventually, the results of the electrochemical and modeling studies were perfectly matched.en_US
dc.identifier.doi10.1007/s00289-023-04727-3
dc.identifier.endpage677en_US
dc.identifier.issn0170-0839
dc.identifier.issn1436-2449
dc.identifier.issue1en_US
dc.identifier.scopus2-s2.0-85148594723en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage661en_US
dc.identifier.urihttps://doi.org/10.1007/s00289-023-04727-3
dc.identifier.urihttps://hdl.handle.net/11616/101180
dc.identifier.volume81en_US
dc.identifier.wosWOS:000939351100001en_US
dc.identifier.wosqualityQ2en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherSpringeren_US
dc.relation.ispartofPolymer Bulletinen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectPhenazopyridineen_US
dc.subjectVoltammetryen_US
dc.subjectBovine serum albuminen_US
dc.subjectMolecular dockingen_US
dc.subjectMolecular dynamics simulationen_US
dc.titleElectrochemical and in silico study of the interaction between phenazopyridine and bovine serum albuminen_US
dc.typeArticleen_US

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