Selective protein immobilization onto gold nanoparticles deposited under vacuum on a protein-repellent self-assembled monolayer

The immobilization of proteins on flat substrates plays an important role for a wide spectrum of applications in the fields of biology, medicine, and biochemistry, among others. An essential prerequisite for the use of proteins (e.g., in biosensors) is the conservation of their biological activity....

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 29(2013), 49 vom: 10. Dez., Seite 15328-35
1. Verfasser: Peissker, Tobias (VerfasserIn)
Weitere Verfasser: Deschaume, Olivier, Rand, Danielle R, Boyen, Hans-Gerd, Conard, Thierry, Van Bael, Margriet J, Bartic, Carmen
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2013
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Gold 7440-57-5
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520 |a The immobilization of proteins on flat substrates plays an important role for a wide spectrum of applications in the fields of biology, medicine, and biochemistry, among others. An essential prerequisite for the use of proteins (e.g., in biosensors) is the conservation of their biological activity. Losses in activity upon protein immobilization can largely be attributed to a random attachment of the proteins to the surface. In this study, we present an approach for the immobilization of proteins onto a chemically heterogeneous surface, namely a surface consisting of protein-permissive and protein-repellent areas, which allows for significant reduction of random protein attachment. As protein-permissive, i.e., as protein-binding sites, ultra pure metallic nanoparticles are deposited under vacuum onto a protein-repellent PEG-silane polymer layer. Using complementary surface characterization techniques (atomic force microscopy, quartz crystal microbalance, and X-ray photoelectron spectroscopy) we demonstrate that the Au nanoparticles remain accessible for protein attachment without compromising the protein-repellency of the PEG-silane background. Moreover, we show that the amount of immobilized protein can be controlled by tuning the Au nanoparticle coverage. This method shows potential for applications requiring the control of protein immobilization down to the single molecule level 
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700 1 |a Deschaume, Olivier  |e verfasserin  |4 aut 
700 1 |a Rand, Danielle R  |e verfasserin  |4 aut 
700 1 |a Boyen, Hans-Gerd  |e verfasserin  |4 aut 
700 1 |a Conard, Thierry  |e verfasserin  |4 aut 
700 1 |a Van Bael, Margriet J  |e verfasserin  |4 aut 
700 1 |a Bartic, Carmen  |e verfasserin  |4 aut 
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