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Scientific result | Nanotoxicology
Researchers from I2BC@Saclay and Iramis, in collaboration with Léon Brillouin laboratory, analyzed the structure of the "corona" of two model proteins adsorbed on silica nanoparticles, by using the small-angle neutron scattering technique. They show that the structures formed are true nano-assemblies, in which the proteins retain their shape.
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.
L Marichal, G Giraudon-Colas, F Cousin, A Thill, J Labarre, Y Boulard, JC Aude, S Pin, JP Renault. Protein−Nanoparticle Interactions: What Are the Protein−Corona Thickness and Organization? (2019) Langmuir, 35 :10831−10837 http://dx.doi.org/10.1021/acs.langmuir.9b01373
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