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Issue 4, 2013
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Protein corona formation for nanomaterials and proteins of a similar size: hard or soft corona?

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Abstract

Nanoparticles (NPs) entering a biological fluid undergo surface modification due to dynamic, physicochemical interactions with biological components, especially proteins. In this work we used complementary bio-physico-chemical approaches to characterize the effects of interactions between CeO2 NPs, immunoglobulins (IgGs) and bovine serum albumin (BSA) of a similar size on protein structural evolution as well as formation of (hetero-) aggregates. Using circular dichroism we showed that IgGs and BSA underwent significant structural changes after interaction with NPs. The NPs and protein–NPs were observed after size exclusion chromatography, highlighting the fact that few aggregates were stable enough to pass this mild separation step. X-ray absorption spectroscopy suggested that the surface chemistry of NPs was not affected by these proteins, also implying weak interactions. Competitive experiments revealed that, while the serum was more concentrated for BSA, IgG–NP aggregates were more stable. Altogether, our results indicate that, under our experimental conditions, the formation of a “protein corona” is an unstable and reversible mechanism. This indicates that, when NPs and proteins are similar in size, the adsorption concept (i.e. protein corona concept) cannot be applied to model the NP–protein interaction, and a heteroaggregation model is more appropriate.

Graphical abstract: Protein corona formation for nanomaterials and proteins of a similar size: hard or soft corona?

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Publication details

The article was received on 17 Jul 2012, accepted on 04 Dec 2012 and first published on 10 Dec 2012


Article type: Paper
DOI: 10.1039/C2NR33611A
Citation: Nanoscale, 2013,5, 1658-1668
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    Protein corona formation for nanomaterials and proteins of a similar size: hard or soft corona?

    W. Liu, J. Rose, S. Plantevin, M. Auffan, J. Bottero and C. Vidaud, Nanoscale, 2013, 5, 1658
    DOI: 10.1039/C2NR33611A

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