By a News Reporter-Staff News Editor at Life Science Weekly -- Researchers detail new data in Proteins. According to news originating from Oak Ridge, Tennessee, by NewsRx correspondents, research stated, "Concern about the toxicity of engineered nanoparticles, such as the prototypical nanomaterial C-60 fullerene, continues to grow. While, evidence continues to mount that C-60 and its derivatives may pose health hazards, the specific molecular interactions of these particles with biological macromolecules require further investigation."
Our news journalists obtained a quote from the research from Oak Ridge National Laboratory, "In this article, we report combined experimental and theoretical studies on the interaction of one of the most prevalent proteins in the human body, human serum albumin (HSA), with C-60 in an aqueous environment. The C-60-HSA interaction was probed by circular dichroism (CD) spectroscopy, small-angle neutron scattering (SANS), and atomistic molecular dynamics (MD) simulations to understand C-60-driven changes in the structure of HSA in solution. The CD spectroscopy demonstrates that the secondary structure of the protein decreases in alpha-helical content in response to the presence of C-60 (0.68 nm in diameter). Similarly, C-60 produces subtle changes in the solution conformation of HSA (an 8.0 nm x 3.8 nm protein), as evidenced by the SANS data and MD simulations, but the data do not indicate that C-60 changes the oligomerization state of the protein, such as by inducing aggregation."
According to the news editors, the research concluded: "The results demonstrate that the interaction is not highly disruptive to the protein in a manner that would prevent it from performing its physiological function."
For more information on this research see: Human serum albumin interactions with C-60 fullerene studied by spectroscopy, small-angle neutron scattering, and molecular dynamics simulations. Journal of Nanoparticle Research, 2013;15(7):181-191. Journal of Nanoparticle Research can be contacted at: Springer, Van Godewijckstraat 30, 3311 Gz Dordrecht, Netherlands. (Springer - www.springer.com; Journal of Nanoparticle Research - www.springerlink.com/content/1388-0764/)
The news correspondents report that additional information may be obtained from S. Li, Oak Ridge Natl Lab, Biol & Soft Matter Div, Oak Ridge, TN 37831, United States. Additional authors for this research include X.C. Zhao, Y.M. Mo, P.T. Cummings and W.T. Heller (see also Proteins).
Keywords for this news article include: Carbon, Physics, Oak Ridge, Tennessee, Fullerenes, United States, Serum Albumin, Blood Proteins, Nanotechnology, Molecular Dynamics, Acute-Phase Proteins, Emerging Technologies, North and Central America
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