title: SANS and UV-vis spectroscopy studies of resultant structure from lysozyme adsorption on silica nanoparticles.
abstract: The interaction of lysozyme protein (M.W. 14.7 kD) with two sizes of silica nanoparticles (16 and 25 nm) has been examined in aqueous solution using UV-vis spectroscopy and small-angle neutron scattering (SANS). The measurements were performed on fixed concentration (1 wt %) of nanoparticles and varying concentration of protein in the range 0 to 2 wt %. The adsorption isotherm as obtained using UV-vis spectroscopy suggests strong interaction of the two components and shows an exponential behavior. The saturation values of adsorption are found to be around 90 and 270 protein molecules per particle for 16 and 25 nm sized nanoparticles, respectively. The adsorption of protein on nanoparticles leads to the aggregation of particles and these structures have been studied by SANS. The aggregates are characterized by fractal structure coexisting with unaggregated particles at low protein concentrations and free proteins at higher protein concentrations. Further, contrast variation SANS measurements have been carried out to differentiate the adsorbed and free protein in these systems.
authors.affiliation: Solid State Physics Division, Bhabha Atomic Research Centre, Trombay, Mumbai 400 085, India.
authors.forename: Sugam
authors.initials: S
authors.lastname: Kumar
authors.forename: Vinod K
authors.initials: VK
authors.lastname: Aswal
authors.forename: Joachim
authors.initials: J
authors.lastname: Kohlbrecher
mesh_terms: D000327:Adsorption; D009113:Muramidase / Q000737:chemistry*; D053758:Nanoparticles / Q000737:chemistry*; D053838:Scattering, Small Angle; D012822:Silicon Dioxide / Q000737:chemistry*; D013056:Spectrophotometry, Ultraviolet
chemical_list: D012822:Silicon Dioxide; D009113:Muramidase