What interactions drive the salivary mucosal pellicle formation?

Gibbins, Hannah L., Yakubov, Gleb E., Proctor, Gordon B., Wilson, Stephen and Carpenter, Guy H. (2014) What interactions drive the salivary mucosal pellicle formation?. Colloids and Surfaces B: Biointerfaces, 120 184-192. doi:10.1016/j.colsurfb.2014.05.020

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Author Gibbins, Hannah L.
Yakubov, Gleb E.
Proctor, Gordon B.
Wilson, Stephen
Carpenter, Guy H.
Title What interactions drive the salivary mucosal pellicle formation?
Journal name Colloids and Surfaces B: Biointerfaces   Check publisher's open access policy
ISSN 0927-7765
Publication date 2014-08-01
Sub-type Article (original research)
DOI 10.1016/j.colsurfb.2014.05.020
Open Access Status DOI
Volume 120
Start page 184
End page 192
Total pages 9
Place of publication Amsterdam, Netherlands
Publisher Elsevier
Language eng
Formatted abstract
• Largely protein showed the ability to bind through hydrophobic interactions, yet some also bind according to their charges.
• The hydrophobic surfaces showed the closest match to the known bound mucosal pellicle.
• Salivary protein binding to particles was improved in some samples when incubated with transglutaminase.

The bound salivary pellicle is essential for protection of both the enamel and mucosa in the oral cavity. The enamel pellicle formation is well characterised, however the mucosal pellicle proteins have only recently been clarified and what drives their formation is still unclear. The aim of this study was to examine the salivary pellicle on particles with different surface properties (hydrophobic or hydrophilic with a positive or negative charge), to determine a suitable model to mimic the mucosal pellicle. A secondary aim was to use the model to test how transglutaminase may alter pellicle formation. Particles were incubated with resting whole mouth saliva, parotid saliva and submandibular/sublingual saliva. Following incubation and two PBS and water washes bound salivary proteins were eluted with two concentrations of SDS, which were later analysed using SDS-PAGE and Western blotting. Experiments were repeated with purified transglutaminase to determine how this epithelial-derived enzyme may alter the bound pellicle. Protein pellicles varied according to the starting salivary composition and the particle chemistry. Amylase, the single most abundant protein in saliva, did not bind to any particle indicating specific protein binding. Most proteins bound through hydrophobic interactions and a few according to their charges. The hydrophobic surface most closely matched the known salivary mucosal pellicle by containing mucins, cystatin and statherin but an absence of amylase and proline-rich proteins. This surface was further used to examine the effect of added transglutaminase. At the concentrations used only statherin showed any evidence of crosslinking with itself or another saliva protein.

In conclusion, the formation of the salivary mucosal pellicle is probably mediated, at least in part, by hydrophobic interactions to the epithelial cell surface.
Keyword Saliva
Hydrophobic forces
Proteins -- analysis
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: School of Chemical Engineering Publications
Official 2015 Collection
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Citation counts: TR Web of Science Citation Count  Cited 14 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 15 times in Scopus Article | Citations
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Created: Wed, 11 Jun 2014, 17:41:40 EST by Gleb Yakubov on behalf of School of Chemical Engineering