Paper Citing NAMD - Abstract
Li, Song; Zhao, Xiongce; Mo, Yiming; Cummings, Peter T.; Heller, William T.
Human serum albumin interactions with C-60 fullerene studied by spectroscopy, small-angle neutron scattering, and molecular dynamics simulations
JOURNAL OF NANOPARTICLE RESEARCH, 15 Art. No. UNSP 1769, JUL 2013
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. 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. 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.
