Bovine Serum Albumin as a Platform for Designing Biologically Active Nanocarriers—Experimental and Computational Studies

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dc.contributor.authorAdamczyk, Olga
dc.contributor.authorSzota, Magdalena
dc.contributor.authorRakowski, Kamil
dc.contributor.authorProchownik, Magdalena
dc.contributor.authorDoveiko, Daniel
dc.contributor.authorChen, Yu
dc.contributor.authorJachimska, Barbara
dc.contributor.organizationDepartment of Physics, Cracow University of Technology, Krakow, Polanden
dc.contributor.organizationJerzy Haber Institute of Catalysis and Surface Chemistry Polish Academy of Sciences, Krakow, Polanden
dc.contributor.organizationDepartment of Physics, University of Strathclyde, Glasgow, UKen
dc.date.accessioned2024-01-23T15:12:13Z
dc.date.available2024-01-23T15:12:13Z
dc.date.issued2023-12-19
dc.description.abstractDue to the specificity of their structure, protein systems are adapted to carry various ligands. The structure of many proteins potentially allows for two types of immobilization of a therapeutic agent, either on the outer surface of the protein or within the protein structure. The existence of two active sites in BSA’s structure, the so-called Sudlow I and II, was confirmed. The conducted research involved determining the effectiveness of BSA as a potential carrier of 5-fluorouracil (5FU). 5-fluorouracil is a broad-spectrum anticancer drug targeting solid tumors. The research was carried out to estimate the physicochemical properties of the system using complementary measurement techniques. The optimization of the complex formation conditions made it possible to obtain significant correlations between the form of the drug and the effective localization of the active substance in the structure of the protein molecule. The presence of two amino groups in the 5FU structure contributes to the deprotonation of the molecule at high pH values (pH > 8) and the transition to the anionic form (AN1 and AN3). To investigate the binding affinity of the tautomeric form with BSA, UV-vis absorption, fluorescence quenching, zeta potential, QCM-D, and CD spectroscopic studies were performed. The experimental research was supported by molecular dynamics (MD) simulations and molecular docking. The simulations confirm the potential location of 5FU tautomers inside the BSA structure and on its surface.en
dc.description.sponsorshipThe presented work was funded by ICSC PAS, Grant NCN OPUS 2021/41/B/ST5/02233.
dc.identifier.citationAdamczyk, O.; Szota, M.; Rakowski, K.; Prochownik, M.; Doveiko, D.; Chen, Y.; Jachimska, B. Bovine Serum Albumin as a Platform for Designing Biologically Active Nanocarriers—Experimental and Computational Studies. Int. J. Mol. Sci. 2024, 25, 37. https://doi.org/10.3390/ijms25010037en
dc.identifier.doi10.3390/ijms25010037
dc.identifier.issn1422-0067
dc.identifier.urihttps://open.icm.edu.pl/handle/123456789/23700
dc.language.isoen
dc.publisherMDPIen
dc.rightsUznanie autorstwa 4.0 Międzynarodowe*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectbovine serum albuminen
dc.subjectfluorouracilen
dc.subjectdrug delivery systemen
dc.subjectligand–protein interactionen
dc.subjectprotein structureen
dc.subjectmolecular dockingen
dc.titleBovine Serum Albumin as a Platform for Designing Biologically Active Nanocarriers—Experimental and Computational Studiesen
dc.typearticleen
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