Journal
ACS NANO
Volume 8, Issue 2, Pages 1871-1877Publisher
AMER CHEMICAL SOC
DOI: 10.1021/nn4063374
Keywords
carbon nanoparticles; fullerene; lysozyme; nanobiotechnology; protein nanoparticle interaction; NMR spectroscopy
Categories
Funding
- Italian Ministero dell'Universita e della Ricerca [RBAP114AMK]
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Integrating carbon nanoparticles (CNPs) with proteins to form hybrid functional assemblies is an innovative research area with great promise for medical, nanotechnology, and materials science. The comprehension of CNP-protein interactions requires the still-missing identification and characterization of the 'binding pocket' for the CNPs. Here, using Lysozyme and C-60 as model systems and NMR chemical shift perturbation analysis, a protein-CNP binding pocket is identified unambiguously in solution and the effect of the binding, at the level of the single amino acid, is characterized by a variety of experimental and computational approaches. Lysozyme forms a stoichiometric 1:1 adduct with C-60 that is dispersed monomolecularly in water. Lysozyme maintains its tridimensional structure upon interaction with C-60 and only a few identified residues are perturbed. The C-60 recognition is highly specific and localized in a well-defined pocket.
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