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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/131396
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dc.contributor.authorOzhukil Kollath, Vinayaraj-
dc.contributor.authorVan den Broeck, Freya-
dc.contributor.authorFehér, Krisztina-
dc.contributor.authorMartins, José C.-
dc.contributor.authorLuyten, Jan-
dc.contributor.authorTraina, Karl-
dc.contributor.authorMullens, Steven-
dc.contributor.authorCloots, Rudi-
dc.date.accessioned2015-12-07T15:34:47Z-
dc.date.accessioned2016-10-25T21:23:26Z-
dc.date.available2015-12-07T15:34:47Z-
dc.date.available2016-10-25T21:23:26Z-
dc.date.issued2015-
dc.identifierhttp://dx.doi.org/10.1002/chem.201500223-
dc.identifier.citationChemistry (weinheim an der Bergstrasse, Germany), v. 21, n. 29, p. 10497-10505, 2015.-
dc.identifier.issn1521-3765-
dc.identifier.urihttp://hdl.handle.net/11449/131396-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/131396-
dc.description.abstractBiocompatible inorganic nano- and microcarriers can be suitable candidates for protein delivery. This study demonstrates facile methods of functionalization by using nanoscale linker molecules to change the protein adsorption capacity of hydroxyapatite (HA) powder. The adsorption capacity of bovine serum albumin as a model protein has been studied with respect to the surface modifications. The selected linker molecules (lysine, arginine, and phosphoserine) can influence the adsorption capacity by changing the electrostatic nature of the HA surface. Qualitative and quantitative analyses of linker-molecule interactions with the HA surface have been performed by using NMR spectroscopy, zeta-potential measurements, X-ray photoelectron spectroscopy, and thermogravimetric analyses. Additionally, correlations to theoretical isotherm models have been calculated with respect to Langmuir and Freundlich isotherms. Lysine and arginine increased the protein adsorption, whereas phosphoserine reduced the protein adsorption. The results show that the adsorption capacity can be controlled with different functionalization, depending on the protein-carrier selections under consideration. The scientific knowledge acquired from this study can be applied in various biotechnological applications that involve biomolecule-inorganic material interfaces.en
dc.format.extent10497-10505-
dc.language.isoeng-
dc.publisherWiley-VCH Verlag GmbH & Co. KGaA, Weinheim-
dc.sourcePubMed-
dc.subjectAdsorptionen
dc.subjectAmino acidsen
dc.subjectNMR spectroscopyen
dc.subjectProteinsen
dc.subjectSurface chemistryen
dc.titleA modular approach to study protein adsorption on surface modified hydroxyapatiteen
dc.typeoutro-
dc.contributor.institutionUniversity of Liège-
dc.contributor.institutionFlemish Institute for Technological Research (VITO)-
dc.contributor.institutionGhent University-
dc.contributor.institutionKatholieke Universiteit Leuven-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.description.affiliationDepartment of Chemistry, University of Liège, Liège, Belgium-
dc.description.affiliationSustainable Materials Management, Flemish Institute for Technological Research (VITO), Boeretang, Mol, Belgium-
dc.description.affiliationDepartment of Organic Chemistry,Ghent University, Ghent, Belgium-
dc.description.affiliationDepartment of Metallurgy and Materials EngineeringKatholieke Universiteit Leuven, Heverlee, Belgium-
dc.description.affiliationAPTIS, University of Liège, Liège, Belgium-
dc.description.affiliationDepartamento de Física, Faculdade de Ciências (FC), Universidade Estadual Paulista (UNESP), Bauru, SP, Brasil-
dc.description.affiliationUnespDepartamento de Física, Faculdade de Ciências (FC), Universidade Estadual Paulista (UNESP), Bauru, SP, Brasil-
dc.identifier.doi10.1002/chem.201500223-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofChemistry (weinheim an der Bergstrasse, Germany)-
dc.identifier.pubmed26096378-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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