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    Self-Assembly/Aggregation Behavior and Adsorption of Enamel Matrix Derivate Protein to Silica Surfaces

    Year: 2006

    Journal: Langmuir 2006, 22, 2227-2234, 20100827

    Authors: Halthur T.J., Björklund A., Elofsson U.M.

    Last authors: Ulla M. Elofsson

    Organizations: YKI, Institute for Surface Chemistry, Box 5607, SE-114 86 Stockholm, Sweden, and Department of Chemistry, Surface Chemistry, Royal Institute of Technology, SE-100 44 Stockholm, Sweden

    Country: Sweden

    Adsorption of the amelogein protein mixture enamel matrix derivate (EMD) to silica surfaces has been studied by in situ ellipsometry and quartz crystal microbalance with dissipation (QCM-D). The protein was found to adsorb as nanospheres in mono- or multilayers, depending on the concentration of “free” nanospheres available in solution. The concentration of free nanospheres is determined by the competitive processes of adsorption and rapid aggregation into microscopic particles, measured by dynamic light scattering (DLS). Multilayers could also be formed by sequential injections of fresh EMD solution. At higher temperature, an up to 6 times thicker gel-like film was formed on the substrate surface, and decreasing the pH lead to disruption of the multilayer/aggregate formation and a decreased amount adsorbed.