Format

Send to

Choose Destination
Nat Commun. 2016 Jun 9;7:11770. doi: 10.1038/ncomms11770.

Dynamic protein coronas revealed as a modulator of silver nanoparticle sulphidation in vitro.

Author information

1
Interdisciplinary Nanoscience Center (iNANO), Aarhus University, Gustav Wieds Vej 14, 8000 Aarhus, Denmark.
2
Department of Public Health, Aarhus University, Bartholins Alle 2, 8000 Aarhus, Denmark.
3
Department of Physics, Aarhus University, Ny Munkegade 120, 8000 Aarhus, Denmark.
4
Department of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej 10, 8000 Aarhus, Denmark.
5
Department of Chemistry, Lomonosov Moscow State University, Leninskie gory 1/3, 119991 Moscow, Russia.

Abstract

Proteins adsorbing at nanoparticles have been proposed as critical toxicity mediators and are included in ongoing efforts to develop predictive tools for safety assessment. Strongly attached proteins can be isolated, identified and correlated to changes in nanoparticle state, cellular association or toxicity. Weakly attached, rapidly exchanging proteins are also present at nanoparticles, but are difficult to isolate and have hardly been examined. Here we study rapidly exchanging proteins and show for the first time that they have a strong modulatory effect on the biotransformation of silver nanoparticles. Released silver ions, known for their role in particle toxicity, are found to be trapped as silver sulphide nanocrystals within the protein corona at silver nanoparticles in serum-containing cell culture media. The strongly attached corona acts as a site for sulphidation, while the weakly attached proteins reduce nanocrystal formation in a serum-concentration-dependent manner. Sulphidation results in decreased toxicity of Ag NPs.

PMID:
27278102
PMCID:
PMC4906166
DOI:
10.1038/ncomms11770
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Nature Publishing Group Icon for PubMed Central
Loading ...
Support Center