Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/342157
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dc.contributor.CRUESPUNIVERSIDADE ESTADUAL DE CAMPINASpt_BR
dc.contributor.authorunicampGaldino, Flávia Elisa-
dc.contributor.authorunicampLoh, Watson-
dc.typeArtigopt_BR
dc.titleEffect of particle functionalization and solution properties on the adsorption of bovine serum albumin and lysozyme onto silica nanoparticlespt_BR
dc.contributor.authorGaldino, F.E.-
dc.contributor.authorPicco, A.S.-
dc.contributor.authorSforca, M.L.-
dc.contributor.authorCardoso, M.B.-
dc.contributor.authorLoh, W.-
dc.subjectAlbuminapt_BR
dc.subjectLisozimapt_BR
dc.subject.otherlanguageAlbuminpt_BR
dc.subject.otherlanguageLysozymept_BR
dc.description.abstractSilica nanoparticles present an enormous potential as controlled drug delivery systems with high selectivity towards diseased cells. This application is directly related to the phenomenon of protein corona, characterized by the spontaneous adsorption of proteins on the nanoparticle surface, which is not fully understood. Here, we report an investigation on the influence of pH, ionic strength and temperature on the thermodynamics of interaction of bovine serum albumin protein (BSA) with non-functionalized silica nanoparticles (SiO2NPs). Complementary, we also investigated the ability of polyethylene glycol (PEG) and zwitterionic sulfobetaine (SBS) surface-modified nanoparticles to prevent the adsorption of BSA (protein negatively charged at physiological pH) and lysozyme (protein positively charged at physiological pH). We showed that BSA interaction with SiO2NPs is enthalpically governed. On the other hand, functionalization of silica nanoparticles with PEG and SBS completely prevented BSA adsorption. However, these functionalized nanoparticles presented a negative zeta potential and were not able to suppress lysozyme anchoring due to strong nanoparticle-protein electrostatic attraction. Due to the similarity of BSA with Human Serum Albumin, this investigation bears a resemblance to processes involved in the phenomenon of protein corona in human blood, producing information that is relevant for the future biomedical use of functionalized nanoparticlespt_BR
dc.relation.ispartofColloids and surfaces. B: biointerfacespt_BR
dc.relation.ispartofabbreviationColloid surf. B: biointerfacespt_BR
dc.publisher.cityAmsterdampt_BR
dc.publisher.countryPaíses Baixospt_BR
dc.publisherElsevierpt_BR
dc.date.issued2020-
dc.date.monthofcirculationFeb.pt_BR
dc.language.isoengpt_BR
dc.description.volume186pt_BR
dc.rightsFechadopt_BR
dc.sourceSCOPUSpt_BR
dc.identifier.issn0927-7765pt_BR
dc.identifier.eissn1873-4367pt_BR
dc.identifier.doi10.1016/j.colsurfb.2019.110677pt_BR
dc.identifier.urlhttps://www.sciencedirect.com/science/article/pii/S0927776519308215pt_BR
dc.date.available2020-05-28T16:03:57Z-
dc.date.accessioned2020-05-28T16:03:57Z-
dc.description.provenanceSubmitted by Cintia Oliveira de Moura (cintiaom@unicamp.br) on 2020-05-28T16:03:57Z No. of bitstreams: 0en
dc.description.provenanceMade available in DSpace on 2020-05-28T16:03:57Z (GMT). No. of bitstreams: 0 Previous issue date: 2020en
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/342157-
dc.contributor.departmentsem informaçãopt_BR
dc.contributor.departmentDepartamento de Físico-químicapt_BR
dc.contributor.unidadeInstituto de Químicapt_BR
dc.contributor.unidadeInstituto de Químicapt_BR
dc.subject.keywordAdsorptionpt_BR
dc.subject.keywordEnzymespt_BR
dc.subject.keywordIonic strengthpt_BR
dc.subject.keywordNanoparticlespt_BR
dc.identifier.source2-s2.0-85075855894pt_BR
dc.creator.orcid0000-0002-7799-3077pt_BR
dc.creator.orcid0000-0002-8049-3321pt_BR
dc.type.formArtigopt_BR
dc.identifier.articleid110677pt_BR
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