Complex fluids containing low concentrations of slender colloidal rods can display a high viscosity, while little flow is needed to thin the fluid. This feature makes slender rods essential constituents in industrial applications and biology. Though this behaviour strongly depends on the rod-length, so far no direct relation could be identified. We employ a library of filamentous viruses to study the effect of rod size and flexibility on the zero-shear viscosity and shear-thinning behaviour. Rheology and small angle neutron 1 arXiv:1910.08349v1 [cond-mat.soft] 18 Oct 2019 scattering data are compared to a revised version of the standard theory for ideally stiff rods, which incorporates a complete shear-induced dilation of the confinement. While the earlier predicted length-independent pre-factor of the restricted rotational diffusion coefficient is confirmed by varying the length and concentration of the rods, the revised theory correctly predicts the shear thinning behaviour as well as the underlying orientational order. These results can be directly applied to understand the manifold systems based on rod-like colloids and design new materials.

In this work, we develop a general theoretical scheme to study tracer-diffusion in mixtures of interacting colloidal particles where the influence of solvent-mediated hydrodynamic interactions is also considered. Based on the many-body Smoluchowski diffusion equation, we derive in a first step an exact microscopic expression of the irreducible memory function ͑self-friction function͒ associated with the self-intermediate scattering function and with the mean squared displacement of a tagged particle. By applying a mode-coupling scheme ͑MCS͒ to the irreducible memory function, we obtain explicit expressions for the tracer-diffusion quantities in terms of partial static structure factors and hydrodynamic functions. The influence of hydrodynamic interactions ͑HI͒ is accounted for using a far-field expansion of the two-body hydrodynamic diffusivity tensors. For charge-stabilized colloids, this is a good approximation due to strong electrostatic repulsion between the particles. Various applications are discussed in order to illustrate the versatility of our mode-coupling scheme.

The colloidal stability of nearly monodisperse aqueous dispersions of rod-shaped gold particles is studied by dynamic light scattering and electrophoresis. The average length of the gold particles is adjusted between 39 and 730 nm, and the diameter is about 17 nm. The translational diffusion coefficients are consistent with calculations for single nonaggregated rods with a 10-15 nm thick poly(vinyl pyrrolidone) (PVP) adsorption layer. This supports the colloidal stability observed. Electrophoresis measurements show that the PVP-stabilized gold rods are negatively charged with a ζ potential of about -47 mV, which according to interaction calculations is sufficient for double-layer stabilization. Gold-sphere dispersions are investigated for comparison. It turns out that PVP-stabilized gold spheres have a ζ potential similar to that of the colloidal rods.

Temperature gradient-induced migration of biomolecules, known as thermophoresis or thermodiffusion, changes upon ligand binding. In recent years, this effect has been used to determine protein-ligand binding constants. The mechanism through which thermodiffusive properties change when complexes are formed, however, is not understood. An important contribution to thermodiffusive properties originates from the thermal response of hydrogen bonds. Because there is a considerable difference between the degree of solvation of the protein-ligand complex and its isolated components, ligand-binding is accompanied by a significant change in hydration. The aim of the present work is therefore to investigate the role played by hydrogen bonding on the change in thermodiffusive behavior upon ligand-binding. As a model system, we use cyclodextrins (CDs) and acetylsalicylic acid (ASA), where quite a significant change in hydration is expected and where no conformational changes occur when a CD/ASA complex is formed in aqueous solution. Thermophoresis was investigated in the temperature range of 10-50 °C by infrared thermal diffusion forced Rayleigh scattering. Nuclear magnetic resonance measurements were performed at 25 °C to obtain information about the structure of the complexes. All CD/ASA complexes show a stronger affinity toward regions of lower temperature compared to the free CDs. We found that the temperature sensitivity of thermophoresis correlates with the 1-octanol/water partition coefficient. This observation not only establishes the relation between thermodiffusion and degree of hydrogen bonding but also opens the possibility to relate thermodiffusive properties of complexes to their partition coefficient, which cannot be determined otherwise. This concept is especially interesting for protein-ligand complexes where the protein undergoes a conformational change, different from the CD/ASA complexes, giving rise to additional changes in their hydrophilicity.