The nano-bio interface mapped by oxidative footprinting of the adsorption sites of myoglobin

Abstract : Oxidative footprinting has been used to study the structure of macromolecular assemblies such as protein-protein and protein-ligand complexes. We propose a novel development of this technique to probe the protein corona that forms at the surface of nanoparticles in any biological medium. Indeed, very few techniques allow studying this interface at the molecular and residue level. Based on hydroxyl radical-mediated oxidation of proteins and analysis by nanoscale liquid chromatography coupled to tandem mass spectrometry (nanoLC-MS/MS), two sites of adsorption of myoglobin on silica nanoparticles are identified. This method gives new insights in the understanding of protein adsorption on nanomaterials.
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Article dans une revue
Analytical and Bioanalytical Chemistry, Springer Verlag, 2014, 406, pp.8037 - 8040. 〈10.1007/s00216-014-8188-7〉
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https://hal-cea.archives-ouvertes.fr/cea-01758749
Contributeur : Serge Palacin <>
Soumis le : mercredi 4 avril 2018 - 17:24:12
Dernière modification le : vendredi 4 mai 2018 - 01:11:09

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Stephanie Devineau, Christelle Mathé, Véronique Legros, Florence Gonnet, Régis Daniel, et al.. The nano-bio interface mapped by oxidative footprinting of the adsorption sites of myoglobin. Analytical and Bioanalytical Chemistry, Springer Verlag, 2014, 406, pp.8037 - 8040. 〈10.1007/s00216-014-8188-7〉. 〈cea-01758749〉

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