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Adsorption from human saliva: time dependence and major components
Malmö högskola, Faculty of Odontology (OD).
Malmö högskola, Faculty of Odontology (OD).ORCID iD: 0000-0003-3173-7577
Malmö högskola, Faculty of Health and Society (HS).
2002 (English)In: Journal of Dental Research Conferens;81, 2002Conference paper, Published paper (Refereed)
Abstract [en]

Objectives: The aims of the present study were to investigate the adsorption from human whole saliva to solid surfaces in terms of dependence of adsorption time and surface wettability, to investigate pellicle elutability with buffer and sodium dodecyl sulphate (SDS) and finally to identify major components involved. Methods: Time resolved in situ ellipsometry was used to determine the adsorbed amounts and adsorption rates from human whole saliva onto pure (hydrophilic) and methylated (hydrophobized) silica surfaces. Two-dimensional gel electrophoresis was used to identify salivary components in the secretions as well as major components in pellicles. Results: The results demonstrated that on hydrophobic surfaces the initial adsorption was rapid and a plateau was reached, whereas on hydrophilic ones a continuous increase was observed during the time course of experiments. Contrary to what was expected, it was found that buffer rinsing removed less material after short adsorption times on hydrophobic surfaces, whereas less time dependence was observed on hydrophilic ones. After SDS exposure a minor fraction remained adsorbed after 15 minutes of adsorption, while a complete removal of the adsorbed film was observed after 2 hours of adsorption on hydrophobic surfaces. On hydrophilic surfaces a minor fraction remained adsorbed after both 15 minutes and 2 hours of adsorption. The two-dimensional gel electrophoresis revealed the presence of more than 50 proteins, with a molecular mass below 200 kDa present in whole saliva. Of these proteins only a few components were detected in the fraction eluted by SDS. Conclusions: We conclude that the different desorbability upon buffer rinsing and addition of SDS indicate that adsorbed proteins have varying binding strengths to the two types of surfaces. The time dependence observed and the compositional analysis show that the adsorbed pellicle undergoes conformational and/or compositional changes.

Place, publisher, year, edition, pages
2002.
National Category
Dentistry
Identifiers
URN: urn:nbn:se:mau:diva-10787Local ID: 4134OAI: oai:DiVA.org:mau-10787DiVA, id: diva2:1407830
Conference
IADR/AADR/CADR General Session, San Diego, California (03/08/2002)
Available from: 2020-02-29 Created: 2020-02-29 Last updated: 2022-06-27Bibliographically approved

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Lindh, LiselottSvensäter, GunnelArnebrant, Thomas

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