The effect of enamel proteins on erosion.

Baumann, Tommy; Saads Carvalho, Thiago; Lussi, Adrian (2015). The effect of enamel proteins on erosion. Scientific Reports, 5, p. 15194. Nature Publishing Group 10.1038/srep15194

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Enamel proteins form a scaffold for growing hydroxyapatite crystals during enamel formation. They are then almost completely degraded during enamel maturation, resulting in a protein content of only 1% (w/v) in mature enamel. Nevertheless, this small amount of remaining proteins has important effects on the mechanical and structural properties of enamel and on the electrostatic properties of its surface. To analyze how enamel proteins affect tooth erosion, human enamel specimens were deproteinated. Surface microhardness (SMH), surface reflection intensity (SRI) and calcium release of both deproteinated and control specimens were monitored while continuously eroding them. The deproteination itself already reduced the initial SMH and SRI of the enamel significantly (p < 0.001 and p < 0.01). During the course of erosion, the progression of all three evaluated parameters differed significantly between the two groups (p < 0.001 for each). The deproteinated enamel lost its SMH and SRI faster, and released more calcium than the control group, but these differences were only significant at later stages of erosion, where not only surface softening but surface loss can be observed. We conclude that enamel proteins have a significant effect on erosion, protecting the enamel and slowing down the progression of erosion when irreversible surface loss starts to occur.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > School of Dental Medicine
04 Faculty of Medicine > School of Dental Medicine > Department of Preventive, Restorative and Pediatric Dentistry
04 Faculty of Medicine > School of Dental Medicine > Restorative Dentistry, Research

UniBE Contributor:

Baumann, Tommy, Saads Carvalho, Thiago, Lussi, Adrian

Subjects:

600 Technology > 610 Medicine & health

ISSN:

2045-2322

Publisher:

Nature Publishing Group

Language:

English

Submitter:

Tommy Baumann

Date Deposited:

24 Nov 2015 10:07

Last Modified:

05 Dec 2022 14:50

Publisher DOI:

10.1038/srep15194

PubMed ID:

26468660

BORIS DOI:

10.7892/boris.73224

URI:

https://boris.unibe.ch/id/eprint/73224

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