Low-fouling properties in serum of carboxylic-oligo(ethylene glycol)-based interfaces
In 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...
| Autores: | , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2021 |
| País: | Brasil |
| Institución: | Universidade Estadual Paulista (UNESP) |
| Repositorio: | Repositório Institucional da UNESP |
| Idioma: | inglés |
| OAI Identifier: | oai:repositorio.unesp.br:11449/210762 |
| Acceso en línea: | http://dx.doi.org/10.1016/j.colsurfa.2021.126426 http://hdl.handle.net/11449/210762 |
| Access Level: | acceso abierto |
| Palabra clave: | Low-fouling interfaces QCM-D Molecular dynamics Protein adsorption Self-assembled monolayers |
| Sumario: | In 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. |
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