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Synthetic nanoparticles of bovine serum albumin with entrapped salicylic acid

dc.contributor.authorBronze-Uhle, E. S. [UNESP]
dc.contributor.authorCosta, B. C. [UNESP]
dc.contributor.authorXimenes, V. F. [UNESP]
dc.contributor.authorLisboa-Filho, P. N. [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2018-12-11T16:45:18Z
dc.date.available2018-12-11T16:45:18Z
dc.date.issued2017-01-01
dc.description.abstractBovine serum albumin (BSA) is highly water soluble and binds drugs or inorganic substances noncovalently for their effective delivery to various affected areas of the body. Due to the well-defined structure of the protein, containing charged amino acids, albumin nanoparticles (NPs) may allow electrostatic adsorption of negatively or positively charged molecules, such that substantial amounts of drug can be incorporated within the particle, due to different albumin-binding sites. During the synthesis procedure, pH changes significantly. This variation modifies the net charge on the surface of the protein, varying the size and behavior of NPs as the drug delivery system. In this study, the synthesis of BSA NPs, by a desolvation process, was studied with salicylic acid (SA) as the active agent. SA and salicylates are components of various plants and have been used for medication with anti-inflammatory, antibacterial, and antifungal properties. However, when administered orally to adults (usual dose provided by the manufacturer), there is 50% decomposition of salicylates. Thus, there has been a search for some time to develop new systems to improve the bioavailability of SA and salicylates in the human body. Taking this into account, during synthesis, the pH was varied (5.4, 7.4, and 9) to evaluate its influence on the size and release of SA of the formed NPs. The samples were analyzed using field-emission scanning electron microscopy, transmission electron microscopy, Fourier transform infrared, zeta potential, and dynamic light scattering. Through fluorescence, it was possible to analyze the release of SA in vitro in phosphate-buffered saline solution. The results of chemical morphology characterization and in vitro release studies indicated the potential use of these NPs as drug carriers in biological systems requiring a fast release of SA.en
dc.description.affiliationDepartment of Physics São Paulo State University (Unesp) School of Sciences
dc.description.affiliationDepartment of Chemistry São Paulo State University (Unesp) School of Sciences
dc.description.affiliationUnespDepartment of Physics São Paulo State University (Unesp) School of Sciences
dc.description.affiliationUnespDepartment of Chemistry São Paulo State University (Unesp) School of Sciences
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipIdFAPESP: 2014/204710
dc.description.sponsorshipIdCNPq: 304810/2010-0
dc.format.extent11-21
dc.identifierhttp://dx.doi.org/10.2147/NSA.S117018
dc.identifier.citationNanotechnology, Science and Applications, v. 10, p. 11-21.
dc.identifier.doi10.2147/NSA.S117018
dc.identifier.issn1177-8903
dc.identifier.lattes1353862414532005
dc.identifier.orcid0000-0002-7734-4069
dc.identifier.scopus2-s2.0-85007603272
dc.identifier.urihttp://hdl.handle.net/11449/169309
dc.language.isoeng
dc.relation.ispartofNanotechnology, Science and Applications
dc.relation.ispartofsjr2,723
dc.rights.accessRightsAcesso restritopt
dc.sourceScopus
dc.subjectAlbumin nanoparticles
dc.subjectDrug delivery
dc.subjectNano-carriers
dc.subjectSalicylic acid entrapped
dc.titleSynthetic nanoparticles of bovine serum albumin with entrapped salicylic aciden
dc.typeArtigopt
dspace.entity.typePublication
relation.isOrgUnitOfPublicationaef1f5df-a00f-45f4-b366-6926b097829b
relation.isOrgUnitOfPublication.latestForDiscoveryaef1f5df-a00f-45f4-b366-6926b097829b
unesp.author.lattes1353862414532005[4]
unesp.author.orcid0000-0002-7734-4069[4]
unesp.campusUniversidade Estadual Paulista (UNESP), Faculdade de Ciências, Baurupt

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