Abstract
Understanding the composition and structure of the acquired enamel pellicle (AEP) has been a major goal in oral biology. Our lab has conducted studies on the composition of AEP formed on permanent enamel. The exhaustive exploration has provided a comprehensive identification of more than 100 proteins from AEP formed on permanent enamel. The AEP formed on deciduous enamel has not been subjected to the same biochemical characterization scrutiny as that of permanent enamel, despite the fact that deciduous enamel is structurally different from permanent enamel. We hypothesized that the AEP proteome and peptidome formed on deciduous enamel may also be composed of unique proteins, some of which may not be common with AEP of permanent enamel explored previously. Pellicle material was collected from 10 children (aged 18–54 months) and subjected to mass spectrometry analysis. A total of 76 pellicle proteins were identified from the deciduous pellicle proteome. In addition, 38 natural occurring AEP peptides were identified from 10 proteins, suggesting that primary AEP proteome/peptidome presents a unique proteome composition. This is the first study to provide a comprehensive investigation of in vivo AEP formed on deciduous enamel.
Highlights
The relationship between human saliva and dental enamel is a complex one, including that of the formation of the acquired enamel pellicle (AEP)
This can be related to the fact that these proteins adsorb strongly to the hydroxyapatite of enamel, and are readily cleaved by proteolytic enzymes found in the oral environment [6,7]
The base-peak chromatogram for reversed-phase chromatography monitored by the mass spectrometer represents the intensity of all peptide ions in the sample in a single scan after trypsin digestion for proteome analysis (Figure 1A), and after centrifugal filtration with molecular weight cut-off (MWCO) < 10 kDa to maintain AEP occurring peptides for peptidome analysis (Figure 1B)
Summary
The relationship between human saliva and dental enamel is a complex one, including that of the formation of the acquired enamel pellicle (AEP). Data collected on the permanent AEP peptidome revealed the presence of multiple protein fragments from histatins, statherin, and acidic PRPs [5,6] This can be related to the fact that these proteins adsorb strongly to the hydroxyapatite of enamel, and are readily cleaved by proteolytic enzymes found in the oral environment [6,7]. The oblique organization of enamel rods and their significantly smaller crystallite deviation result in a clear and quantifiable difference between the surface and subsurface crystallite orientation in deciduous teeth [11]. A generally similar pattern in the amount of the amino acids has been seen, the amino acids glycine, serine, and tyrosine were reported in statistically significantly different quantities in the two types of AEP [13] This suggests that the pellicles may have different protein compositions. We hypothesize that the proteome and peptidome of human deciduous in vivo AEP will present a unique protein profile
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