The news correspondents obtained a quote from the research, "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."
According to the news reporters, the research concluded: "This method shows potential for applications requiring the control of protein immobilization down to the single molecule level."
For more information on this research see: Selective protein immobilization onto gold nanoparticles deposited under vacuum on a protein-repellent self-assembled monolayer. Langmuir, 2013;29(49):15328-35. (
Our news journalists report that additional information may be obtained by contacting T. Peissker,
Keywords for this news article include: Leuven,
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