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- DOI: 10.1039/b916773k
- PMID: 20135034
- UKPMCID: 20135034
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Site-selective immobilisation of functional enzymes on to polystyrene nanoparticles.
Wong, Lu Shin; Okrasa, Krzysztof; Micklefield, Jason
Organic & Biomolecular Chemistry. 2010;8(4):782-787.
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Full-text held externally
- DOI: 10.1039/b916773k
- PMID: 20135034
- UKPMCID: 20135034
Abstract
The immobilisation of proteins on to nanoparticles has a number of applications ranging from biocatalysis through to cellular delivery of biopharmaceuticals. Here we describe a phosphopantetheinyl transferase (Sfp)-catalysed method for immobilising proteins bearing a small 12-mer "ybbR" tag on to nanoparticles functionalised with coenzyme A. The Sfp-catalysed immobilisation of proteins on to nanoparticles is a highly efficient, single step reaction that proceeds under mild conditions and results in a homogeneous population of proteins that are covalently and site-specifically attached to the surface of the nanoparticles. Several enzymes of interest for biocatalysis, including an arylmalonate decarboxylase (AMDase) and a glutamate racemase (GluR), were immobilised on to nanoparticles using this approach. These enzymes retained their activity and showed high operational stability upon immobilisation.