Structure of the 'protein corona' for Human Serum Albumin-Silica nanoparticles
The "protein corona" phenomenon has been invoked to explain the presence of cryptic epitopes - immunologically recognisable peptide strands - when proteins are mixed with nanoparticles. Its structure is not known. Our focus is the surface and bulk structure of complexes between human serum albumin and 20nm silica particles. On FIGARO, our previous experiments at the air-water interface showed that the silica-protein layer structure was well fitted by a three-layer model and by merging the bottom and the second layers the composition equations could be solved for mass concentrations of the three components. On D11, data have been fitted by a “beads on a string” model and the extent of protein “coating” of the nanoparticle (as proposed for the “corona”) is not yet proven. Here our aim is to add the missing contrasts needed to resolve the structure of the air-water interface (FIGARO) and resolve the lowest protein concentration required to induce aggregation of a small fraction of the silica (D11). This will be achieved because we will use fully deuterated human serum albumin (for the first time): its availability from the DLAB will allow us to write up the work for publication.
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WHITE John W.; Richard A. Campbell; JACKSON Andrew; LINDNER Peter; RAYNES Jared and SEBASTIANI Federica. (2013). Structure of the 'protein corona' for Human Serum Albumin-Silica nanoparticles. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.9-13-486
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