The role of enamel proteins in protecting mature human enamel against acidic environments: a double layer force spectroscopy study.

Biointerphases

Nanotechnology and Integrated Bioengineering Centre (NIBEC), School of Engineering, University of Ulster, Shore Road, Newtownabbey, Co., Antrim, BT37 0QB, Northern Ireland, UK.

Published: December 2012

Characterisation of the electrostatic properties of dental enamel is important for understanding the interfacial processes that occur on a tooth surface and how these relate to the natural ability of our teeth to withstand chemical attack from the acids in many soft drinks. Whereas, the role of the mineral component of the tooth enamel in providing this resistance to acid erosion has been studied extensively, the influence of proteins that are also present within the structure is not well understood. In this paper, we report for the first time the use of double-layer force spectroscopy to directly measure electrostatic forces on as received and hydrazine-treated (deproteinated) enamel surfaces in solutions with different pH to determine how the enamel proteins influence acid erosion surface potential and surface charge of human dental enamel. The deproteination of the treated samples was confirmed by the loss of the amide bands (~1,300-1,700 cm(-1)) in the FTIR spectrum of the sample. The force characteristics observed were found to agree with the theory of electrical double layer interaction under the assumption of constant potential and allowed the surface charge per unit area to be determined for the two enamel surfaces. The values and, importantly, the sign of these adsorbed surface charges indicates that the protein content of dental enamel contributes significantly to the electrostatic double layer formation near the tooth surface and in doing so can buffer the apatite crystals against acid attack. Moreover, the electrostatic interactions within this layer are a driving factor for the mineral transfer from the tooth surface and the initial salivary pellicle formation.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4875143PMC
http://dx.doi.org/10.1007/s13758-011-0014-6DOI Listing

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