C60@Lysozyme: direct observation by nuclear magnetic resonance of a 1:1 fullerene protein adduct.
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 C60 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 C60 that is dispersed monomolecularly in water. Lysozyme maintains its tridimensional structure upon interaction with C60 and only a few identified residues are perturbed. The C60 recognition is highly specific and localized in a well-defined pocket.
Dipartimento di Chimica "G. Ciamician", Alma Mater Studiorum Università di Bologna , via F. Selmi 2, 40126 Bologna, Italy.
Matteo
M
Calvaresi
Fabio
F
Arnesano
Sara
S
Bonacchi
Andrea
A
Bottoni
Vincenza
V
Calò
Stefano
S
Conte
Giuseppe
G
Falini
Simona
S
Fermani
Maurizio
M
Losacco
Marco
M
Montalti
Giovanni
G
Natile
Luca
L
Prodi
Francesca
F
Sparla
Francesco
F
Zerbetto
D002850:Chromatography, Gel; D005453:Fluorescence; D037741:Fullerenes / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D009113:Muramidase / Q000737:chemistry*; D013056:Spectrophotometry, Ultraviolet
D037741:Fullerenes; D009113:Muramidase; C069837:fullerene C60