Study of the protein corona formed by the ad- sorption of hemoproteins on silica nanoparticles

Laurent Marichal (1) , J.-P Renault (1) , Fabrice Cousin (2) , S. Combet (2) , A Gatin (1) , J.-C Aude (3) , Y Boulard (3) , J Labarre (3) , Serge Pin (1)

1 LIONS - Laboratoire Interdisciplinaire sur l'Organisation Nanométrique et Supramoléculaire
2 LLB - UMR 12 - Laboratoire Léon Brillouin
3 I2BC - Institut de Biologie Intégrative de la Cellule

The performance of a bio-nanomaterial essentially results from interactions that occur at its surface and that depend on the adsorption of biomolecules, particularly proteins. In order to improve the biocompatibility of nanomaterials, one of the challenges is to understand the mechanisms of protein adsorption and to appreciate the modifications of adsorbed proteins. Using model hemoproteins and monodisperse silica nanopar-ticles (SiNPs) we studied the impact of the protein size on its ability to interact on the silica surface in a qualitative and quantitative way. Adsorption differences between myo-globin and hemoglobin (Devineau et al ., Langmuir, 2017) were previously investigated and we decided to extend the comparison to even larger hemoproteins that can be regarded as oligomeric hemoglobins. We studied the hemopro-tein/SiNPs interactions using a panel of methods: adsorption isotherms, circular dichroism, small angle neutron scattering , and isothermal titration calorimetry. The end result of this study is that the protein size can have a major impact in terms of global affinity towards a silica surface but also in terms of protein structure alteration and thermodynamic changes caused by the adsorption.

Domains: Material chemistry

Laurent Marichal, J.-P Renault, Fabrice Cousin, S. Combet, A Gatin, et al.. Study of the protein corona formed by the ad- sorption of hemoproteins on silica nanoparticles. 19th International Union for Pure and Applied Biophysics Congress, Jul 2017, Edinburgh, United Kingdom. ⟨cea-02339188⟩