The interaction of the globular protein lysozyme with silica nanoparticles of diameter 20 nm was studied in a pH range between the isoelectric points (IEPs) of silica and the protein (pH 3-11). The adsorption affinity and capacity of lysozyme on the silica particles is increasing progressively with pH, and the adsorbed protein induces bridging aggregation of the silica particles. Structural properties of the aggregates were studied as a function of pH at a fixed protein-to-silica concentration ratio which corresponds to a surface concentration of protein well below a complete monolayer in the complete-binding regime at pH > 6. Sedimentation studies indicate the presence of compact aggregates at pH 4-6 and a loose flocculated network at pH 7-9, followed by a sharp decrease of aggregate size near the IEP of lysozyme. The structure of the bridged silica aggregates was studied by cryo-transmission electron microscopy (cryo-TEM) and small-angle X-ray scattering. The structure factor S(q) derived from the scattering profiles displays characteristic features of particles interacting by a short-range attractive potential and can be represented by the square-well Percus-Yevick potential model, with a potential depth not exceeding 3k(B)T.

Charge-driven bridging of nanoparticles by macromolecules represents a promising route for engineering functional structures, but the strong electrostatic interactions involved when using conventional polyelectrolytes impart irreversible complexation and ill-defined structures. Recently it was found that the electrostatic interaction of silica nanoparticles with small globular proteins leads to aggregate structures that can be controlled by pH. Here we study the combined influence of pH and electrolyte concentration on the bridging aggregation of silica nanoparticles with lysozyme in dilute aqueous dispersions. We find that protein binding to the silica particles is determined by pH irrespective of the ionic strength. The hetero-aggregate structures formed by the silica particles with the protein were studied by small-angle X-ray scattering (SAXS) and the structure factor data were analyzed on the basis of a short-range square-well attractive pair potential (close to the sticky-hard-sphere limit). It is found that the electrolyte concentration has a strong influence on the stickiness near pH 5, where the weakly charged silica particles are bridged by the strongly charged protein. An even stronger influence of the electrolyte is found in the vicinity of the isoelectric point of the protein (pI ¼ 10.7) and is attributed to shielding of the repulsion between the highly charged silica particles and hydrophobic interactions between the bridging protein molecules.

The adsorption of lysozyme and ß-lactoglobulin onto silica nanoparticles (diameter 21 nm) was studied in the pH range 2–11 at three different ionic strengths. Since the two proteins have a widely different isoelectric point (pI), electrostatic interactions with the negative silica surface lead to a different dependence of adsorption on pH. For lysozyme (pI ≈ 11), the adsorption level increases with pH and reaches a value corresponding to about two close-packed monolayers at pH = pI. In the multilayer adsorption region near pI, added electrolyte causes a decrease in adsorption, which is attributed to the screening of attractive interactions between protein molecules in the first and second adsorbed layer. For ß-lactoglobulin (pI ≈ 5), a pronounced maximum of the adsorbed amount is found at pH 4 in the absence of salt. It is attributed to the adsorption of oligomers of the protein that exist in the solution at this pH. An inversion in the influence of salt on the adsorbed amount occurs at pH > pI, where the protein and the surface are both negatively charged. This inversion is attributed to the screening of the repulsive protein-surface and protein–protein interactions. The adsorption isotherms were analyzed with the Guggenheim–Anderson–De Boer (GAB) model, which allows for two adsorption states (strongly and weakly bound protein).

The neutron capture rate on 15 N may be of considerable importance for s-process nucleosynthesis in red giants as well as for the nucleosynthesis in inhomogeneous big bang scenarios. We measured the reaction cross section of 15 N(n,␥) 16 N at the Forschungszentrum Karlsruhe with a fast cyclic neutron activation technique at laboratory neutron energies of 25, 152, and 370 keV. Direct capture and shell model calculations were performed to interpret the results. The presented reaction rate is 30-50 % smaller than the previously used theoretical rates.

The influence of particle size and a surface modifier on the self-assembly of the nonionic surfactant C 12 E 5 at silica nanoparticles was studied by adsorption measurements and small-angle neutron scattering (SANS). Silica nanoparticles of diameter 13 to 43 nm were synthesized involving the basic amino acid lysine. A strong decrease of the limiting adsorption of C 12 E 5 with decreasing particle diameter was found. To unveil the role of lysine as a surface modifier for the observed size dependence of surfactant adsorption, the morphology of the surfactant aggregates assembled on pure siliceous nanoparticles (Ludox-TMA, 27 nm) and their evolution with increasing lysine concentration at a fixed surfactant-to-silica ratio was studied by SANS. In the absence of lysine, the surfactant forms surface micelles at silica particles. As the concentration of lysine is increased, a gradual transition from the surface micelles to detached wormlike micelles in the bulk solution is observed. The changes in surfactant aggregate morphology cause pronounced changes of the system properties, as is demonstrated by turbidity measurements as a function of temperature. These findings are discussed in terms of particle surface curvature and surfactant binding strength, which present new insight into the delicate balance between the two properties.