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 “fr...
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Published in | Langmuir Vol. 22; no. 5; pp. 2227 - 2234 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Washington, DC
American Chemical Society
28.02.2006
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Subjects | |
Online Access | Get full text |
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Summary: | 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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Bibliography: | istex:55C9FD0A7D5FD01CC7A31642EDA5C3F2B42004E0 ark:/67375/TPS-S4HJKMDC-K ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0743-7463 1520-5827 1520-5827 |
DOI: | 10.1021/la0525123 |