Abstract
In biological fluids, an adsorption layer of proteins, a “protein corona” forms around nanoparticles (NPs) largely determining their biological identity. In many interactions with NPs proteins can undergo structural changes. Here, we study the adsorption of insulin onto gold NPs (mean hydrodynamic particle diameter 80 ± 18 nm), focusing on the structural consequences of the adsorption process for the protein. We use surface enhanced Raman scattering (SERS) spectroscopy to study changes in the protein’s secondary structure as well as the impact on integrity and conformations of disulfide bonds immediately on the NP surface. A detailed comparison to SERS spectra of cysteine and cystine provides first mechanistic insights into the causes for these conformational changes. Potential biological and toxicological implications of these findings are also discussed.
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Acknowledgments
The authors acknowledge support of this work by the “Deutsche Forschungsgemeinschaft (DFG)” within the priority programme “Bio-Nano-Responses” (SPP1313). The authors thank S. Schlücker and R. Zellner (both University of Duisburg-Essen) for valuable discussions. LT acknowledges support by a Young Scientists Grant of the UDE, by a research grant of the Centre for Water and Environmental Science (CWE) and by the Bruno-Werdelmann Foundation.
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Grass, S., Treuel, L. Mechanistic aspects of protein corona formation: insulin adsorption onto gold nanoparticle surfaces. J Nanopart Res 16, 2254 (2014). https://doi.org/10.1007/s11051-014-2254-0
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DOI: https://doi.org/10.1007/s11051-014-2254-0