ABSTRACT
Typical characterization of nanoparticle dispersion and compounding processes by dynamic light scattering (DLS) and TEM lack quantitative information on fractal structure, aggregation number, and specific surface area. In this work a synchrotron ultra-small-angle X-ray scattering (USAXS) investigation on diffusion flame and 'Aerosil' silica powders, as well as on their desagglomeration by high-pressure liquid dispersion (200-1400 bar) is presented. Primary particle size, polydispersity, and specific surface area are measured for powders, stirred-in dispersions, and after high-pressure processing with identical results, showing the in-situ applicability of USAXS. These parameters, as well as the hard aggregate mass fractal dimension, with typically Df = 2.15 representing reaction-limited cluster aggregation, are determined by synthesis process conditions. They are unchanged even at the highest hydrodynamic stresses; thus, neither comminution nor agglomerate restructuring nor re-agglomeration occurs. Fragmentation reflects in decreasing radii of gyration, which are compared to mobility equivalent radii from DLS in agreement with theory.
ABSTRACT
The microstructure-dependence of dip-coated particulate thin films on the stability of an aqueous silica sol used as coating bath is studied. Different stability conditions are adjusted in the sol by changing electrolyte concentration and pH value. Care was taken to avoid pronounced aggregation of the particles before the coating process. The characterization of the stability behavior gives clear evidence of a non-DLVO contribution at low pH values that is attributed to hydration forces. Structural evolution of the particulate network during film formation is studied using a dialysis accumulation procedure. The viscosity of the accumulated sol is measured as a function of shear rate and related to the drying characteristic of the coating process. Atomic force microscopy (AFM), small-angle X-ray scattering (SAXS) and N2 sorption are used to obtain information on the surface and volume structure of the dip-coated films. The structure of coatings is found to distinctly vary with stability parameters. This is attributed to changing interactions during the first drying stage. Finally, the influence of coating structures on the light transmission properties is determined. A comparison between the extinction of the uncoated and the coated substrate revealed a difference of up to +/-50% in dependence on the microstructure.
ABSTRACT
We use small-angle x-ray scattering (SAXS) as a tool to study the binding of proteins to spherical polyelectrolyte brushes (SPB) in situ. The SPB consists of a solid core of approximately 100 nm diam onto which long polyelectrolyte chains [poly(styrene sulfonic acid, PSS) and poly(acrylic acid, PAA)] have been densely grafted. The proteins used in this investigation, Bovine Serum Albumine (BSA) and Bovine Pancreatic Ribonuclease A (RNase A), adsorb strongly to these SPB if the ionic strength is low despite their negative charge. Virtually no adsorption takes place at high ionic strength. SAXS demonstrates that both proteins are distributed within the brush. The findings reported here give further evidence that the strong adsorption of proteins to SPB is due to the "counterions release forces": The patches of positive charge on the surface of the proteins become multivalent counterions of the polyelectrolyte chains. Thus, a concomitant number of co- and counterions is thereby released and the entropy of the entire system is increased. The repulsive Coulombic interaction as well as the steric repulsion between the proteins and the brush layer are counterbalanced by this effect. The data discussed here demonstrate that the adsorption of proteins in SPB presents a new principle for the immobilization of proteins.
