Well dispersed fractal aggregates as filler in polymer-silica nanocomposites: long range effects in rheology

We are presenting a new method of processing polystyrene-silica nanocomposites, which results in a very well-defined dispersion of small primary aggregates (assembly of 15 nanoparticles of 10 nm diameter) in the matrix. The process is based on a high boiling point solvent, in which the nanoparticles are well dispersed, and controlled evaporation. The filler's fine network structure is determined over a wide range of sizes, using a combination of Small Angle Neutron Scattering (SANS) and Transmission Electronic Microscopy (TEM). The mechanical response of the nanocomposite material is investigated both for small (ARES oscillatory shear and Dynamical Mechanical Analysis) and large deformations (uniaxial traction), as a function of the concentration of the particles. We can investigate the structure-property correlations for the two main reinforcement effects: the filler network contribution, and a filler-polymer matrix effect. Above a silica volume fraction threshold, we see a divergence of the modulus correlated to the build up of a connected network. Below the threshold, we obtain a new additional elastic contribution of much longer terminal time than the matrix. Since aggregates are separated by at least 60 nm, this new filler-matrix contribution cannot be described solely with the concept of glassy layer (2nm)

Critical structure factor in Ising systems

We perform a large-scale Monte Carlo simulation of the three-dimensional Ising model on simple cubic lattices of size L^3 with L=128 and 256. We determine the corresponding structure factor (Fourier transform of the two-point function) and compare it with several approximations and with experimental results. We also compute the turbidity as a function of the momentum of the incoming radiation, focusing in particular on the deviations from the Ornstein-Zernicke expression of Puglielli and Ford.Comment: 16 page

Multiple Scale Reorganization of Electrostatic Complexes of PolyStyrene Sulfonate and Lysozyme

We report on a SANS investigation into the potential for these structural reorganization of complexes composed of lysozyme and small PSS chains of opposite charge if the physicochemical conditions of the solutions are changed after their formation. Mixtures of solutions of lysozyme and PSS with high matter content and with an introduced charge ratio [-]/[+]intro close to the electrostatic stoichiometry, lead to suspensions that are macroscopically stable. They are composed at local scale of dense globular primary complexes of radius ~ 100 {\AA}; at a higher scale they are organized fractally with a dimension 2.1. We first show that the dilution of the solution of complexes, all other physicochemical parameters remaining constant, induces a macroscopic destabilization of the solutions but does not modify the structure of the complexes at submicronic scales. This suggests that the colloidal stability of the complexes can be explained by the interlocking of the fractal aggregates in a network at high concentration: dilution does not break the local aggregate structure but it does destroy the network. We show, secondly, that the addition of salt does not change the almost frozen inner structure of the cores of the primary complexes, although it does encourage growth of the complexes; these coalesce into larger complexes as salt has partially screened the electrostatic repulsions between two primary complexes. These larger primary complexes remain aggregated with a fractal dimension of 2.1. Thirdly, we show that the addition of PSS chains up to [-]/[+]intro ~ 20, after the formation of the primary complex with a [-]/[+]intro close to 1, only slightly changes the inner structure of the primary complexes. Moreover, in contrast to the synthesis achieved in the one-step mixing procedure where the proteins are unfolded for a range of [-]/[+]intro, the native conformation of the proteins is preserved inside the frozen core

Structural analysis of haemoglobin binding by HpuA from the Neisseriaceae family

The Neisseriaceae family of bacteria causes a range of diseases including meningitis, septicaemia, gonorrhoea and endocarditis, and extracts haem from haemoglobin as an important iron source within the iron-limited environment of its human host. Herein we report crystal structures of apo- and haemoglobin-bound HpuA, an essential component of this haem import system. The interface involves long loops on the bacterial receptor that present hydrophobic side chains for packing against the surface of haemoglobin. Interestingly, our structural and biochemical analyses of Kingella denitrificans and Neisseria gonorrhoeae HpuA mutants, although validating the interactions observed in the crystal structure, show how Neisseriaceae have the fascinating ability to diversify functional sequences and yet retain the haemoglobin binding function. Our results present the first description of HpuA’s role in direct binding of haemoglobin

Universal ratios of critical amplitudes for the shear viscosity

An analysis of the available shear viscosity data for the critical mixture of water and isobutyric acid gives amplitude ratios in agreement with the theoretical prediction of Peliti.L'analyse des mesures de viscosité existant déjà pour le mélange binaire, d'acide isobutyrique et d'eau donne des rapports d'amplitudes correspondant aux prévisions théoriques de Peliti