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Journal articles

Protein–Nanoparticle Interactions: What Are the Protein–Corona Thickness and Organization?

Laurent Marichal 1 Gaël Giraudon--Colas 1 Fabrice Cousin 2 Antoine Thill 1 Jean Labarre 3 yves Boulard 3 Jean-Christophe Aude 3 Serge Pin 1 Jean-Philippe Renault 1 
1 LIONS - Laboratoire Interdisciplinaire sur l'Organisation Nanométrique et Supramoléculaire
NIMBE UMR 3685 - Nanosciences et Innovation pour les Matériaux, la Biomédecine et l'Energie (ex SIS2M)
2 MMB - LLB - Matière molle et biophysique
LLB - UMR 12 - Laboratoire Léon Brillouin : IRAMIS/LLB/MMB
Abstract : Protein adsorption on a surface is generally evaluated in terms of the evolution of the proteins’ structures and functions. However, when the surface is that of a nanoparticle, the protein corona formed around it possesses a particular supramolecular structure that gives a “biological identity” to the new object. Little is known about the actual shape of the protein corona. Here, the protein corona formed by the adsorption of model proteins (myoglobin and hemoglobin) on silica nanoparticles was studied. Small-angle neutron scattering and oxygenation studies were combined to assess both the structural and functional impacts of the adsorption on proteins. Large differences in the oxygenation properties could be found while no significant global shape changes were seen after adsorption. Moreover, the structural study showed that the adsorbed proteins form an organized yet discontinuous monolayer around the nanoparticles.
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Submitted on : Tuesday, August 27, 2019 - 5:33:37 PM
Last modification on : Sunday, June 26, 2022 - 2:40:26 AM



Laurent Marichal, Gaël Giraudon--Colas, Fabrice Cousin, Antoine Thill, Jean Labarre, et al.. Protein–Nanoparticle Interactions: What Are the Protein–Corona Thickness and Organization?. Langmuir, American Chemical Society, 2019, 35 (33), pp.10831-10837. ⟨10.1021/acs.langmuir.9b01373⟩. ⟨cea-02272503⟩



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