17 resultados para discotics, columar liquid crystals, solid-state NMR, liquid crystal engineering


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Two conjugated oligomers, representing elementary segments of fluorene-thiophene copolymers, are compared in terms of the microscopic morphology and the optical properties of thin deposits. The atomic force microscopy morphological data and the solid-state absorption and emission spectra are interpreted in terms of the assembly of the conjugated molecules. The compound with a terthiophene central unit and fluorene end-groups shows well-defined monolayer-by-monolayer assembly into micrometer-long stripe-like structures, with a crystalline herringbone-type organization within the monolayers. Polarized confocal microscopy indicates a strong orientation of the crystalline domains within the stripes. In contrast, the compound with a terfluorene central unit and thiophene end groups forms no textured aggregates and the optical spectra in the solid-state are very similar to those recorded in solution, suggesting that the molecules interact only weakly in the solid. The difference in behaviour between the two compounds most probably originates from their different capability to form densely-packed assemblies of interacting π-systems.

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Nanoconfined synthesized crystalline fullerene mesoporous carbon (C60-FMC) with bimodal pore architectures of 4.95 nm and 10-15 nm pore sizes characterized by XRD, TEM, nitrogen adsorption/ desorption isotherm and solid-state NMR, and the material was used for protein immobilization. The solid-state 13C NMR spectrum of C60-FMC along with XRD, BET and TEM confirms the formation of fullerene mesoporous carbon structure C60-FMC. The immobilization of albumin (from bovine serum, BSA) protein biomolecule in a buffer solution at pH 4.7 was used to determine the adsorption properties of the C60-FMC material and its structural changes investigated by FT-IR. We demonstrated that the C60-FMC with high surface area and pore volumes have excellent adsorption capacity towards BSA protein molecule. Protein adsorption experiments clearly showed that the C60-FMC with bimodal pore architectures (4.95 nm and 10-15 nm) are suitable material to be used for protein adsorption