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

Author

Listed:
  • Teodora Miclăuş

    (Interdisciplinary Nanoscience Center (iNANO), Aarhus University)

  • Christiane Beer

    (Aarhus University)

  • Jacques Chevallier

    (Aarhus University)

  • Carsten Scavenius

    (Aarhus University)

  • Vladimir E. Bochenkov

    (Interdisciplinary Nanoscience Center (iNANO), Aarhus University
    Lomonosov Moscow State University)

  • Jan J. Enghild

    (Aarhus University)

  • Duncan S. Sutherland

    (Interdisciplinary Nanoscience Center (iNANO), Aarhus University)

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.

Suggested Citation

  • Teodora Miclăuş & Christiane Beer & Jacques Chevallier & Carsten Scavenius & Vladimir E. Bochenkov & Jan J. Enghild & Duncan S. Sutherland, 2016. "Dynamic protein coronas revealed as a modulator of silver nanoparticle sulphidation in vitro," Nature Communications, Nature, vol. 7(1), pages 1-10, September.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms11770
    DOI: 10.1038/ncomms11770
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