RNA-binding proteins are a major target of silica nanoparticles in cell extracts

Upon contact with biological fluids, nanoparticles (NPs) are readily coated by cellular compounds, particularly proteins, which are determining factors for the localization and toxicity of NPs in the organism. Here, we improved a methodological approach to identify proteins that adsorb on silica NPs...

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Bibliographic Details
Published in:Nanotoxicology 2016-12, Vol.10 (10), p.1555-1564
Main Authors: Klein, Géraldine, Mathé, Christelle, Biola-Clier, Mathilde, Devineau, Stéphanie, Drouineau, Emilie, Hatem, Elie, Marichal, Laurent, Alonso, Béatrice, Gaillard, Jean-Charles, Lagniel, Gilles, Armengaud, Jean, Carrière, Marie, Chédin, Stéphane, Boulard, Yves, Pin, Serge, Renault, Jean-Philippe, Aude, Jean-Christophe, Labarre, Jean
Format: Article
Language:English
Subjects:
A549 Cells
Adsorption
Cell Extracts - chemistry
Chemical Sciences
Humans
intrinsically disordered protein
Material chemistry
Nanoparticles
Nanoparticles - chemistry
Nanoparticles - toxicity
Particle Size
Peptide Chain Initiation, Translational
Protein Conformation
Protein corona
Proteins
Proteomics
RNA binding protein
RNA, Fungal - chemistry
RNA-Binding Proteins - chemistry
RNA-Binding Proteins - ultrastructure
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - ultrastructure
silica nanoparticles
Silicon Dioxide - chemistry
Silicon Dioxide - toxicity
Surface Properties
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Summary:Upon contact with biological fluids, nanoparticles (NPs) are readily coated by cellular compounds, particularly proteins, which are determining factors for the localization and toxicity of NPs in the organism. Here, we improved a methodological approach to identify proteins that adsorb on silica NPs with high affinity. Using large-scale proteomics and mixtures of soluble proteins prepared either from yeast cells or from alveolar human cells, we observed that proteins with large unstructured region(s) are more prone to bind on silica NPs. These disordered regions provide flexibility to proteins, a property that promotes their adsorption. The statistical analyses also pointed to a marked overrepresentation of RNA-binding proteins (RBPs) and of translation initiation factors among the adsorbed proteins. We propose that silica surfaces, which are mainly composed of Si-O − and Si-OH groups, mimic ribose-phosphate molecules (rich in -O − and -OH) and trap the proteins able to interact with ribose-phosphate containing molecules. Finally, using an in vitro assay, we showed that the sequestration of translation initiation factors by silica NPs results in an inhibition of the in vitro translational activity. This result demonstrates that characterizing the protein corona of various NPs would be a relevant approach to predict their potential toxicological effects.
ISSN:1743-5390
1743-5404
DOI:10.1080/17435390.2016.1244299