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

DSpace Repository

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

Overview

Detailed record

dc.contributor.author Svendsen, Ida
dc.contributor.author Lindh, Liselott
dc.contributor.author Arnebrant, Thomas
dc.date.accessioned 2007-01-05T01:45:39Z
dc.date.available 2007-01-05T01:45:39Z
dc.date.issued 2006
dc.identifier.citation 157-166
dc.identifier.issn 0927-7765
dc.identifier.uri http://hdl.handle.net/2043/3247
dc.description.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. en
dc.language.iso eng en
dc.publisher Elsevier en
dc.subject Lactoferrin en
dc.subject Lactoperoxidase en
dc.subject Lysozyme en
dc.subject Histatin 5 en
dc.subject Pellicle en
dc.subject.classification Sciences en
dc.title Adsorption behaviour and surfactant elution of cationic salivary proteins at solid/liquid interfaces, studied by in situ ellipsometry en
dc.type Article, peer reviewed scientific en
dc.identifier.paperprint 0 en
dc.contributor.department Malmö University. Faculty of Odontology en
dc.contributor.department Malmö University. Faculty of Health and Society en
dc.identifier.doi 10.1016/j.colsurfb.2006.08.016
dc.subject.srsc Research Subject Categories::NATURAL SCIENCES::Chemistry::Physical chemistry::Surface and colloid chemistry Research Subject
dc.relation.ispartofpublication Colloids and Surfaces B: Biointerfaces;2
dc.relation.ispartofpublicationvolume 53
 Find Full text Files for download
Icon

This item appears in the following Collection(s)

Overview

Search


Browse

My Account

Statistics