Document Type
Article
Publication Date
1-11-2016
Abstract
The response of living systems to nanoparticles is thought to depend on the protein corona, which forms shortly after exposure to physiological fluids and which is linked to a wide array of pathophysiologies. A mechanistic understanding of the dynamic interaction between proteins and nanoparticles and thus the biological fate of nanoparticles and associated proteins is, however, often missing mainly due to the inadequacies in current ensemble experimental approaches. Through the application of a variety of single molecule and single particle spectroscopic techniques in combination with ensemble level characterization tools, we identified different interaction pathways between gold nanorods and bovine serum albumin depending on the protein concentration. Overall, we found that local changes in protein concentration influence everything from cancer cell uptake to nanoparticle stability and even protein secondary structure. We envision that our findings and methods will lead to strategies to control the associated pathophysiology of nanoparticle exposure in vivo.
Language
English
Publication Title
ACS Nano
Rights
© 2016 American Chemical Society. Users may access, download, copy, display and redistribute articles as well as adapt, translate, text and data mine content contained in articles for non-commercial research and education purposes only, and subject to ACS full conditions of use.
Recommended Citation
Dominguez-Medina, S., Kisley, L., Tauzin, L. J., Hoggard, A., Shuang, B., DS Indrasekara, A. S., ... & Link, S. (2016). Adsorption and unfolding of a single protein triggers nanoparticle aggregation. ACS nano, 10(2), 2103-2112.
Manuscript Version
Final Publisher Version