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Please use this identifier to cite or link to this item: http://hdl.handle.net/1942/16184

Title: Selective Protein Immobilization onto Gold Nanoparticles Deposited under Vacuum on a Protein-Repellent Self-Assembled Mono layer
Authors: Peissker, Tobias
Deschaume, Olivier
Rand, Danielle R.
BOYEN, Hans-Gerhard
Conard, Thierry
Van Bael, Margriet J.
Bartic, Carmen
Issue Date: 2013
Citation: LANGMUIR, 29 (49), p. 15328-15335
Abstract: 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.
URI: http://hdl.handle.net/1942/16184
DOI: 10.1021/la403016q
ISI #: 000328437000024
ISSN: 0743-7463
Category: A1
Type: Journal Contribution
Validation: ecoom, 2015
Appears in Collections: Research publications

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