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 &qu...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 22(2006), 5 vom: 28. Feb., Seite 2227-34
1. Verfasser: Halthur, Tobias J (VerfasserIn)
Weitere Verfasser: Björklund, Anna, Elofsson, Ulla M
Format: Aufsatz
Sprache:English
Veröffentlicht: 2006
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Amelogenin Coated Materials, Biocompatible Dental Enamel Proteins Multiprotein Complexes enamel matrix proteins Silicon Dioxide 7631-86-9
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520 |a 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 
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650 4 |a Research Support, Non-U.S. Gov't 
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650 7 |a Coated Materials, Biocompatible  |2 NLM 
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700 1 |a Elofsson, Ulla M  |e verfasserin  |4 aut 
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