Low-fouling properties in serum of carboxylic-oligo(ethylene glycol)-based interfaces

Registro completo de metadados
MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversidade Estadual Paulista (Unesp)-
Autor(es): dc.creatorSantos, Adriano [UNESP]-
Autor(es): dc.creatorGarcia Nicholson, Melany Isabel [UNESP]-
Autor(es): dc.creatorFeliciano, Gustavo Troiano [UNESP]-
Autor(es): dc.creatorBueno, Paulo Roberto [UNESP]-
Data de aceite: dc.date.accessioned2022-02-22T01:07:22Z-
Data de disponibilização: dc.date.available2022-02-22T01:07:22Z-
Data de envio: dc.date.issued2021-06-26-
Data de envio: dc.date.issued2021-06-26-
Data de envio: dc.date.issued2021-06-05-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1016/j.colsurfa.2021.126426-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/210762-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/210762-
Descrição: dc.descriptionIn the present work we evaluated the low-fouling feature of a carboxylic-oligo(ethylene glycol) self-assembled monolayer (carboxylic-OEG-SAM) interface using a quartz crystal microbalance with dissipation monitoring (QCM-D). QCM-D measurements allowed us to estimate the amount of protein loading in two different serum dilutions at two different interfaces: bare gold and carboxylic-OEG. The observed amount of protein adsorbed onto bare gold is about twice higher that of carboxylic OEG interface, confirming the low-fouling characteristics of OEG-modified surfaces. Additionally, QCM-D results demonstrated the existence of two protein adsorption regimes, a faster and a slower, with distinct dissipation energies which was modelled by a two-step kinetic model. The faster regime was attributed to the adsorption of proteins into free sites of the carboxylic-OEG-SAM in a rigid binding process, followed by a slower and more viscoelastic adsorption process ascribed to structural conformational changes; this slower step conforms with the filling of remaining free sites associated with the steric hindrance in which protein-protein interactions defines the slower rate constant for the adsorption.-
Descrição: dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
Descrição: dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)-
Descrição: dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
Descrição: dc.descriptionUniv Estadual Paulista, Inst Chem, Sao Paulo State Univ, BR-14800060 Araraquara, SP, Brazil-
Descrição: dc.descriptionUniv Estadual Paulista, Inst Chem, Sao Paulo State Univ, BR-14800060 Araraquara, SP, Brazil-
Descrição: dc.descriptionCAPES: 88887.463447/2019-00-
Descrição: dc.descriptionFAPESP: 2017/24839-0-
Formato: dc.format6-
Idioma: dc.languageen-
Publicador: dc.publisherElsevier B.V.-
Relação: dc.relationColloids And Surfaces A-physicochemical And Engineering Aspects-
???dc.source???: dc.sourceWeb of Science-
Palavras-chave: dc.subjectLow-fouling interfaces-
Palavras-chave: dc.subjectQCM-D-
Palavras-chave: dc.subjectMolecular dynamics-
Palavras-chave: dc.subjectProtein adsorption-
Palavras-chave: dc.subjectSelf-assembled monolayers-
Título: dc.titleLow-fouling properties in serum of carboxylic-oligo(ethylene glycol)-based interfaces-
Tipo de arquivo: dc.typelivro digital-
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