title: Protein interaction with hydrated C60 fullerene in aqueous solutions.
abstract: 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.
authors.affiliation: Institute of Biology, Karelian Research Center, RAS, 185610 Petrozavodsk, Russia. rozhkov@krc.karelia.ru
authors.forename: S P
authors.initials: SP
authors.lastname: Rozhkov
authors.forename: A S
authors.initials: AS
authors.lastname: Goryunov
authors.forename: G A
authors.initials: GA
authors.lastname: Sukhanova
authors.forename: A G
authors.initials: AG
authors.lastname: Borisova
authors.forename: N N
authors.initials: NN
authors.lastname: Rozhkova
authors.forename: G V
authors.initials: GV
authors.lastname: Andrievsky
mesh_terms: 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
chemical_list: D037741:Fullerenes; D012709:Serum Albumin; D012996:Solutions; D014867:Water; C069837:fullerene C60