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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