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G Brotons

Publications and source records attributed to G Brotons.

3 recordsLinked to original sources

Quantitative SAXS analysis of the P123/water/ethanol ternary phase diagram.

The ternary phase diagram of the amphiphilic triblock copolymer PEO-PPO-PEO ((EO)(20)(PO)(70)(EO)(20) commercialized under the generic name P123), water, and ethanol has been investigated at constant temperature (T = 23 degrees C) by small-angle X-ray scattering (SAXS). The microstructure resulting from the self-assembly of the PEO-PPO-PEO block copolymer varies from micelles in solution to various types of liquid crystalline phases such as cubic, 3D hexagonal close packed spheres (HCPS), 2D hexagonal, and lamellar when the concentration of the polymer is increased. In the isotropic liquid phase, the micellar structural parameters are obtained as a function of the water-ethanol ratio and block copolymer concentration by fitting the scattering data to a model involving core-shell form factor and a hard sphere structure factor of interaction. The micellar core, the aggregation number, and the hard sphere interaction radius decrease when increasing the ethanol/water ratio in the mixed solvent. We show that the fraction of ethanol present in the core is responsible for the swelling of the PPO blocks. In the different liquid crystalline phases, structural parameters such as lattice spacing, interfacial area of PEO block, and aggregation number are also evaluated. In addition to classical phases such as lamellar, 2D hexagonal, and liquid isotropic phases, we have observed a two-phase region in which cubic Fm3m and P6(3)mmc (hexagonally close packing of spheres (HCPS)) phases coexist. This appears at 30% (w/w) of P123 in pure water and with 5% (w/w) of ethanol. At 10% (w/w) ethanol, only the HCPS phase remains present.

Crystallization↗

SARS coronavirus E protein in phospholipid bilayers: an x-ray study.

We investigated the structure of the hydrophobic domain of the severe acute respiratory syndrome E protein in model lipid membranes by x-ray reflectivity and x-ray scattering. In particular, we used x-ray reflectivity to study the location of an iodine-labeled residue within the lipid bilayer. The label imposes spatial constraints on the protein topology. Experimental data taken as a function of protein/lipid ratio P/L and different swelling states support the hairpin conformation of severe acute respiratory syndrome E protein reported previously. Changes in the bilayer thickness and acyl-chain ordering are presented as a function of P/L, and discussed in view of different structural models.

Dimyristoylphosphatidylcholine↗

Hole nucleation in thin diblock copolymer films.

This paper reports an experimental study of a homogeneous nucleation process in the direct space, using an atomic-force microscope. Nucleated patterns are holes in a thin diblock copolymer film. The formation of nuclei from the metastable majority phase is followed either by the dissolution or by the growth of the hole. It is also preceded by the unexpected presence of a bump at the free surface. From the study of the nucleus surface topography at different stages of the evolution, we infer a description of the nucleation mechanism at a molecular level. It involves the existence of ordered metastable states characterized by the presence of compressed internal layers, the formation of pores in the center of the film, and the existence of interfacial flows across these pores. The presence of compressed internal layers was directly demonstrated using Neutron Reflectivity experiments, Our scheme is also consistent with all existing experimental data. After hole nucleation, we identify two distinct growth regimes: the first one is individual and the second one is interactive.

Journal Article↗