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Time Evolution of the Nanoparticle Protein Corona

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† Institut Català de Nanotecnologia, Bellaterra, Barcelona, Spain
‡ Department of Molecular Biology, University of Salzburg, Salzburg, Austria
§ Institut Català de Recerca i Estudis Avançats (ICREA), Barcelona, Spain
* Address correspondence to [email protected]
Cite this: ACS Nano 2010, 4, 7, 3623–3632
Publication Date (Web):June 16, 2010
https://doi.org/10.1021/nn901372t
Copyright © 2010 American Chemical Society
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    Abstract

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    In this work, we explore the formation of the protein corona after exposure of metallic Au nanoparticles (NPs), with sizes ranging from 4 to 40 nm, to cell culture media containing 10% of fetal bovine serum. Under in vitro cell culture conditions, zeta potential measurements, UV−vis spectroscopy, dynamic light scattering and transmission electron microscope analysis were used to monitor the time evolution of the inorganic NP−protein corona formation and to characterize the stability of the NPs and their surface state at every stage of the experiment. As expected, the red-shift of the surface plasmon resonance peak, as well as the drop of surface charge and the increase of the hydrodynamic diameter indicated the conjugation of proteins to NPs. Remarkably, an evolution from a loosely attached toward an irreversible attached protein corona over time was observed. Mass spectrometry of the digested protein corona revealed albumin as the most abundant component which suggests an improved biocompatibility.

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    Table of the complete physicochemical characterization of the NPs used in this work; TEM images of 10 nm AuNPs as synthesized and after incubation in CCM and size distribution; surface charge evolution of different [NPs]/[CCM02] ratios and after different incubation times; surface charge evolution of different [NPs]/[CCM03] ratios and after different incubation times; mass spectroscopy after tryptic digestion of the AuNP-hard corona; characterization of the conjugates of AuNPs with MUA and AUT. This material is available free of charge via the Internet at http://pubs.acs.org.

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