Both an experimental and a theoretical investigation of the fracture propagation mechanisms acting at the process zone scale in glassy polymers are presented. The main aim is to establish a common modeling for different kinds of glassy polymers presenting either steady-state fracture propagation or stick-slip fracture propagation or both, depending on loading conditions and sample shape. On the experimental point of view, new insights are provided by in-situ AFM measurements of the viscoplastic strain fields acting within the micrometric process zone in a brittle epoxy resin, which highlight an extremely slow unexpected steadystate regime with finite plastic strains of about 30% around a blunt crack tip, and accompanied by propagating shear lips. On the theoretical point of view, we apply to glassy polymers some recently developed models for describing soft dissipative fracture that are pertinent with the observed finite strains. We propose a unified modeling of the fracture energy for both the steady-state and stick-slip fracture propagation based on the evaluation of the energy dissipation density at a characteristic strain rate induced in the process zone by the competition between the crack propagation velocity and the macroscopic sample loading rate.

The binary phase diagram of γ-gliadin, a wheat storage protein, in water was explored thanks to the microevaporator, an original PDMS microfluidic device. This protein, usually qualified as insoluble in aqueous environments, displayed a partial solubility in water. Two liquid phases, a very dilute and a dense phase, were identified after a few hours of accumulation time in the microevaporator. This liquid–liquid phase separation (LLPS) was further characterized through in situ micro-Raman spectroscopy of the dilute and dense protein phases. Micro-Raman spectroscopy showed a specific orientation of phenylalanine residues perpendicular to the PDMS surfaces only for the diluted phase. This orientation was ascribed to the protein adsorption at interfaces, which would act as nuclei for the growth of dense phase in bulk. This study, thanks to the use of both aqueous solvent and a microevaporator, would provide some evidence for a possible physicochemical origin of the gliadin assembly in the endoplasmic reticulum of albumen cells, leading to the formation of dense phases called protein bodies. The microfluidic tool could be used also in food science to probe protein–protein interactions in order to build up phase diagrams

In the design of medium and low voltage equipment such as cable accessories, generator, motor end windings or bushings, issues with electrical field enhancement occur at interfaces between insulators and conductors, resulting in accelerated material ageing. The purpose of this paper is to present a novel dielectric composite material which has the properties to mitigate this local amplification. It is a functional dielectric which resistivity decreases by several orders with electric field from 10(14) to 10(9) ohm m up to 1 kV mm(-1) while the dielectric constant decreases from 15 to 12 in the 10(-2)-10(6) Hz range. This novel material is made with graphite nanoplatelets. It may be used as a resistive or capacitive field grading material in electrical applications.

Understanding the complex structure of polymer blends filled with nanoparticles (NPs) is the key to designing their macroscopic properties. Here, the spatial distribution of hydrogenated (H) and deuterated (D) polymer chains asymmetric in mass is studied by small-angle neutron scattering. Depending on the chain mass, a qualitatively new large-scale organization of poly(vinyl acetate) chains beyond the random-phase approximation is evidenced in nanocomposites with attractive polymersilica interactions. The silica is found to systematically induce bulk segregation. Only with long H-chains, a strong scattering signature is observed in the q-range of the NP size: it is the sign of interfacial isotopic enrichment, i.e., of contrasted polymer shells close to the NP surface. A quantitative model describing both the bulk segregation and the interfacial gradient (over ca. 10-20 nm depending on the NP size) is developed, showing that both are of comparable strength. In all cases, NP surfaces trap the polymer blend in a non-equilibrium state, with preferential adsorption around NPs only if chain length and isotopic preference towards the surface combine their entropic and enthalpic driving forces. This structural evidence for interfacial polymer gradients will open the road to quantitative understanding of the dynamics of many-chain nanocomposite systems.

The present paper deals with the correlation between intramolecular and intermolecular interactions of polycarboxybetaines. The degree of coupling between the opposite charges within the polycarboxybetaine molecules was varied by spacers of different length and bythe substitution of additional alkyl chains at the quaternary nitrogen atom. In order to check intermolecular interactions between polycarboxybetaines, SANS measurements were carried out at aqueous polycarboxybetaines solutions. For getting information about the interaction with an oppositely charged polyelectrolyte, multilayers were formed by alternating adsorption of polystyrene sulfonate (PSS) and polycarboxybetaines from aqueous solutions. The occurrence of a structure peak in SANS spectra and the ability to form polyelectrolytemultilayers provide an indicator for the polyelectrolyte character of some of the studied polycarboxybetaines. Not only the charge but also the hydrophobicity of the polycarboxybetaines has a pronounced effect on the chain conformation and therefore on the thickness of the polyelectrolyte multilayers. The results show that small differences in molecular architecture lead to pronounced differences in intermolecular interactions.

Aggregation mechanisms of amyloid β peptides depend on multiple intrinsic and extrinsic physicochemical factors (e.g., peptide chain length, truncation, peptide concentration, pH, ionic strength, temperature, metal concentration, etc.). Due to this high number of parameters, the formation of oligomers and their propensity to aggregate make the elucidation of this physiopathological mechanism a challenging task. From the analytical point of view, up to our knowledge, few techniques are able to quantify, in real time, the proportion and the size of the different soluble species during the aggregation process. This work aims at demonstrating the efficacy of the modern Taylor dispersion analysis (TDA) performed in capillaries (50 μm i.d.) to unravel the speciation of β-amyloid peptides in low-volume peptide samples (∼100 μL) with an analysis time of ∼3 min per run. TDA was applied to study the aggregation process of Aβ(1-40) and Aβ(1-42) peptides at physiological pH and temperature, where more than 140 data points were generated with a total volume of ∼1 μL over the whole aggregation study (about 0.5 μg of peptides). TDA was able to give a complete and quantitative picture of the Aβ speciation during the aggregation process, including the sizing of the oligomers and protofibrils, the consumption of the monomer, and the quantification of different early- and late-formed aggregated species.

The adsorption of a sunflower protein extract at two air− water and oil−water interfaces is investigated using tensiometry, dilational viscoelasticity, and ellipsometry. For both interfaces, a three step mechanism was evidenced thanks to master curve representations of the data taken at different aging times and protein concentrations. At short times, a diffusion limited adsorption of proteins at interfaces is demonstrated. First, a two-dimensional protein film is formed with a partition of the polypeptide chains in the two phases that depends strongly on the nature of the hydrophobic phase: most of the film is in the aqueous phase at the air−water interface, while it is mostly in the organic phase at the oil−water interface. Then a three-dimensional saturated monolayer of proteins is formed. At short times, adsorption mechanisms are analogous to those found with typical globular proteins, while strong divergences are observed at longer adsorption times. Following the saturation step, a thick layer expands in the aqueous phase and appears associated with the release of large objects in the bulk. The kinetic evolution of this second layer is compatible with a diffusion limited adsorption of the minor population of polymeric complexes with hydrodynamic radius R H ∼ 80 nm, evidenced in equilibrium with hexameric globulins (R H ∼ 6 nm) in solution. These complexes could result from the presence of residual polyphenols in the extract and raise the question of the role of these compounds in the interfacial properties of plant protein extracts.