Protein interaction with hydrated C60 fullerene in aqueous solutions

Physicochemical effects of hydrated C(60) fullerenes (HyFn) on serum albumin molecules were studied using ESR spin labeling and differential scanning microcalorimetry. Molecular-colloidal solution of hydrated C(60) fullerenes and their small spherical fractal clusters in water (C(60)FWS), was shown...

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Veröffentlicht in:	Biochemical and biophysical research communications 2003-04, Vol.303 (2), p.562-566
Hauptverfasser:	Rozhkov, S P, Goryunov, A S, Sukhanova, G A, Borisova, A G, Rozhkova, N N, Andrievsky, G V
Format:	Artikel
Sprache:	eng
Schlagworte:	Calorimetry - methods Electron Spin Resonance Spectroscopy Fullerenes - chemistry Humans Protein Conformation Serum Albumin - chemistry Solutions Water
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Zusammenfassung:	Physicochemical effects of hydrated C(60) fullerenes (HyFn) on serum albumin molecules were studied using ESR spin labeling and differential scanning microcalorimetry. Molecular-colloidal solution of hydrated C(60) fullerenes and their small spherical fractal clusters in water (C(60)FWS), was shown to stabilize protein hydration, and decrease specific surface energy in water-protein matrix in salt solutions. The mechanism of HyFn interaction with protein is discussed in terms of HyFn induced formation of protein clusters and phase transition of hydration water.
ISSN:	0006-291X
DOI:	10.1016/S0006-291X(03)00392-9