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 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.
Rozhkov
S P
SP
Institute of Biology, Karelian Research Center, RAS, 185610 Petrozavodsk, Russia. rozhkov@krc.karelia.ru
Goryunov
A S
AS
Sukhanova
G A
GA
Borisova
A G
AG
Rozhkova
N N
NN
Andrievsky
G V
GV
D002151:Calorimetry / Q000379:methods; D004578:Electron Spin Resonance Spectroscopy; D037741:Fullerenes / Q000737:chemistry*; D006801:Humans; D011487:Protein Conformation; D012709:Serum Albumin / Q000737:chemistry*; D012996:Solutions; D014867:Water
D037741:Fullerenes; D012709:Serum Albumin; D012996:Solutions; D014867:Water; C069837:fullerene C60