Self-assembly/aggregation behavior and adsorption of enamel matrix derivate protein to silica surfaces
2006 (English)In: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 22, no 5, 2227-2234 p.Article in journal (Refereed) Published
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 multi layer/aggregate formation and a decreased amount adsorbed.
Place, publisher, year, edition, pages
2006. Vol. 22, no 5, 2227-2234 p.
Adsorption, Crystals, Light scattering, Proteins, Quartz, Silica, Dynamic light scattering (DLS), Enamel matrix derivate (EMD), Gel-like films, Multilayer/aggregate formation
IdentifiersURN: urn:nbn:se:kth:diva-8919DOI: 10.1021/la0523123ISI: 000235744500043ScopusID: 2-s2.0-33644905268OAI: oai:DiVA.org:kth-8919DiVA: diva2:14405
QC 20101019. Uppdaterad från submitted till published (20101019). Tidigare titel: Self-assembly/Aggregation Behavior, and Adsorption of Enamel Matrix Derivate Protein Nanospheres to Silica Surfaces