title: Interferences of Silica Nanoparticles in Green Fluorescent Protein Folding Processes.
abstract: We investigated the relationship between unfolded proteins, silica nanoparticles and chaperonin to determine whether unfolded proteins could stick to silica surfaces and how this process could impair heat shock protein activity. The HSP60 catalyzed green fluorescent protein (GFP) folding was used as a model system. The adsorption isotherms and adsorption kinetics of denatured GFP were measured, showing that denaturation increases GFP affinity for silica surfaces. This affinity is maintained even if the surfaces are covered by a protein corona and allows silica NPs to interfere directly with GFP folding by trapping it in its unstructured state. We determined also the adsorption isotherms of HSP60 and its chaperonin activity once adsorbed, showing that SiO2 NP can interfere also indirectly with protein folding through chaperonin trapping and inhibition. This inhibition is specifically efficient when NPs are covered first with a layer of unfolded proteins. These results highlight for the first time the antichaperonin activity of silica NPs and ask new questions about the toxicity of such misfolded proteins/nanoparticles assembly toward cells.
authors.affiliation: NIMBE, CEA/DSM/IRAMIS et UMR3685 CNRS, CEA-Saclay, Gif sur Yvette, France.|Service de Biologie Intégrative et Génétique Moléculaire, iBiTec-S, FRE3377 CEA-CNRS-Université Paris-Sud, CEA-Saclay, Gif sur Yvette, France.
authors.forename: Géraldine
authors.initials: G
authors.lastname: Klein
authors.affiliation: NIMBE, CEA/DSM/IRAMIS et UMR3685 CNRS, CEA-Saclay, Gif sur Yvette, France.
authors.forename: Stéphanie
authors.initials: S
authors.lastname: Devineau
authors.affiliation: Service de Biologie Intégrative et Génétique Moléculaire, iBiTec-S, FRE3377 CEA-CNRS-Université Paris-Sud, CEA-Saclay, Gif sur Yvette, France.
authors.forename: Jean Christophe
authors.initials: JC
authors.lastname: Aude
authors.affiliation: Service de Bioénergétique, Biologie Structurale et Mécanismes, iBiTec-S, UMR 9198 CEA-CNRS-Université Paris-Sud, CEA-Saclay, Gif sur Yvette, France.
authors.forename: Yves
authors.initials: Y
authors.lastname: Boulard
authors.affiliation: Laboratoire de Chimie Physique, UMR 8000, CNRS-Université Paris-Sud, Orsay, France.
authors.forename: Hélène
authors.initials: H
authors.lastname: Pasquier
authors.affiliation: Service de Biologie Intégrative et Génétique Moléculaire, iBiTec-S, FRE3377 CEA-CNRS-Université Paris-Sud, CEA-Saclay, Gif sur Yvette, France.
authors.forename: Jean
authors.initials: J
authors.lastname: Labarre
authors.affiliation: NIMBE, CEA/DSM/IRAMIS et UMR3685 CNRS, CEA-Saclay, Gif sur Yvette, France.
authors.forename: Serge
authors.initials: S
authors.lastname: Pin
authors.affiliation: NIMBE, CEA/DSM/IRAMIS et UMR3685 CNRS, CEA-Saclay, Gif sur Yvette, France.
authors.forename: Jean Philippe
authors.initials: JP
authors.lastname: Renault
mesh_terms: D049452:Green Fluorescent Proteins / Q000737:chemistry*; D053758:Nanoparticles / Q000737:chemistry*; D017510:Protein Folding; D012822:Silicon Dioxide / Q000737:chemistry*
chemical_list: D049452:Green Fluorescent Proteins; D012822:Silicon Dioxide