Co-adsorption vs. complexation of protein and surfactant in the tubular pores of SBA-15 silica
The interaction of surfactants with adsorbed protein layers is of practical relevance in the context of surface cleaning and the removal of protein from the surface of porous separation membranes. Here we propose to investigate the assembly of the cationic surfactant DPC in the cylindrical pores of SBA-15 (pore width ~ 8 nm) in the presence of pre-adsorbed lysozyme. We will address the question how the processes of co-adsorption, complexation, or displacement of proteins with surfactants are affected by confined geometry of the narrow pores. In preceding studies we have used SANS to determine the morphology of surfactant aggregates adsorbed in the periodic cylindrical pores of SBA-15 silica. The scattering data were analyzed on the basis of a sum of two independent contributions: Bragg scattering (from the ordered pore lattice) and diffused scattering (from spatial correlations) among surfactant aggregates. A similar model will be used to analyze the changes induced by the presence of preadsorbed protein in the pores. From our earlier experience we expect that instrument D16 is ideally suited for studying the co-assembly of lysozyme with the cationic surfactant DPC in nanopores.
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FINDENEGG Gerhard; BHARTI Bhuvnesh; CRISTIGLIO Viviana and MEISSNER Jens. (2013). Co-adsorption vs. complexation of protein and surfactant in the tubular pores of SBA-15 silica. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.9-10-1329
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