Adsorption behaviour and surfactant elution of cationic salivary proteins at solid/liquid interfaces, studied by in situ ellipsometry

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Adsorption behaviour and surfactant elution of cationic salivary proteins at solid/liquid interfaces, studied by in situ ellipsometry

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Publication Article, peer reviewed scientific
Title Adsorption behaviour and surfactant elution of cationic salivary proteins at solid/liquid interfaces, studied by in situ ellipsometry
Author(s) Svendsen, Ida ; Lindh, Liselott ; Arnebrant, Thomas
Date 2006
English abstract
Adsorption of the cationic salivary proteins lactoferrin, lactoperoxidase, lysozyme and histatin 5 to pure (hydrophilic) and methylated (hydrophobized) silica surfaces was investigated by in situ ellipsometry. Effects of concentration (≤10 μg ml−1, for lysozyme ≤200 μg ml−1) and dependence of surface wettability, as well as adsorption kinetics and elutability of adsorbed films by buffer and sodium dodecyl sulphate (SDS) solutions were investigated. Results showed that the amounts adsorbed decreased in the order lactoferrin ≥ lactoperoxidase > lysozyme ≥ histatin 5. On hydrophilic silica, the adsorption was most likely driven by electrostatic interactions, which resulted in adsorbed amounts of lactoferrin that indicated the formation of a monolayer with both side-on and end-on adsorbed molecules. For lactoperoxidase the adsorbed amounts were somewhat higher than an end-on monolayer, lysozyme adsorption showed amounts corresponding to a side-on monolayer, and histatin 5 displayed adsorbed amounts in the range of a side-on monolayer. On hydrophobized substrata, the adsorption was also mediated by hydrophobic interactions, which resulted in lower adsorbed amounts of lactoferrin and lactoperoxidase; closer to side-on monolayer coverage. For both lysozyme and histatin 5 the adsorbed amounts were the same as on the hydrophilic silica. The investigated proteins exhibited fast adsorption kinetics, and the initial kinetics indicated mass transport controlled behaviour at low concentrations on both types of substrates. Buffer rinsing and SDS elution indicated that the proteins in general were more tightly bound to the hydrophobized surface compared to hydrophilic silica. Overall, the surface activity of the investigated proteins implicates their importance in the salivary film formation.
DOI http://dx.doi.org/doi:10.1016/j.colsurfb.2006.08.016 (link to publisher's fulltext)
Publisher Elsevier
Host/Issue Colloids and Surfaces B: Biointerfaces;2
Volume 53
ISSN 0927-7765
Pages 157-166
Language eng (iso)
Subject(s) Lactoferrin
Lactoperoxidase
Lysozyme
Histatin 5
Pellicle
Sciences
Research Subject Categories::NATURAL SCIENCES::Chemistry::Physical chemistry::Surface and colloid chemistry Research Subject
Handle http://hdl.handle.net/2043/3247 (link to this page)

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