Self-assembly/aggregation behavior and adsorption of enamel matrix derivate protein to silica surfaces.
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.
YKI, Institute for Surface Chemistry, Box 5607, SE-114 86 Stockholm, Sweden. tobias.halthur@surfchem.kth.se
Tobias J
TJ
Halthur
Anna
A
Björklund
Ulla M
UM
Elofsson
D000327:Adsorption; D053523:Amelogenin / Q000737:chemistry; D000818:Animals; D020099:Coated Materials, Biocompatible; D003746:Dental Enamel Proteins / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D046912:Multiprotein Complexes; D012822:Silicon Dioxide; D020349:Surface Plasmon Resonance; D013499:Surface Properties; D013552:Swine; D013696:Temperature
D053523:Amelogenin; D020099:Coated Materials, Biocompatible; D003746:Dental Enamel Proteins; D046912:Multiprotein Complexes; C109069:enamel matrix proteins; D012822:Silicon Dioxide