HIGH YIELD SYNTHESIS OF PROTEIN IMPRINTED NANOGELS PREPARED AND PROBED USING MAGNETIC TEMPLATES
2Department of Chemistry and Biomedical Sciences, linnaeus university
3Chemistry Department, College of Science and Engineering, University of Leicester
W describe an approach to the high yield synthesis and assay of protein imprinted nanogels employing templates attached to magnetic carriers.1 The proteolytic enzymes trypsin and pepsin were immobilized on aminofunctionalized solgel coated magnetic nanoparticles. Lightly crosslinked fluorescently doped polyacrylamide nanogels were subsequently produced by high dilution polymerization of monomers in presence of protein-conjugated nanoparticles. This was followed by multiple washes of the magnetically trapped particles and collection of each fraction. Finally a wash of the particles at elevated temperature led to elution of fluorescent nanogel taken on to further characterisation. The nanogels were characterised by a competitive fluorescence assay employing the identical protein conjugated nanoparticles as ligands to reversibly immobilize the corresponding nanogels. Both nanogels exhibited high affinity for their respective target protein and minor crossreactivity for the reference enzyme. This agrees with affinities reported for solid phase synthesized nanogels prepared using low surface area glass bead supports.2
- Berghaus, M., Mohammadi, R. & Sellergren, B. Productive encounter: molecularly imprinted nanoparticles prepared using magnetic templates. Chemical Communications 2014, 50, 8993-8996
- Guerreiro A. et al. Influence of Surface-Imprinted Nanoparticles on Trypsin Activity. Adv Healthc Mater. 2014, 3, 1426-1429
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