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Self-assembly/aggegation behavior, and adsorption of enamel matrix derivate protein to silica surfaces
YKI – Ytkemiska institutet.
2006 (English)In: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 22, p. 2227-2234Article in journal (Refereed)
Abstract [en]

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.

Place, publisher, year, edition, pages
2006. Vol. 22, p. 2227-2234
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Natural Sciences
Identifiers
URN: urn:nbn:se:ri:diva-27153OAI: oai:DiVA.org:ri-27153DiVA: diva2:1054157
Note
A1776Available from: 2016-12-08 Created: 2016-12-08 Last updated: 2017-11-29Bibliographically approved

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