Abstract
Acquired enamel pellicle (AEP) is a protein film that forms on the enamel surface of teeth by selective adsorption of proteins and peptides present in the mouth. This protein film forms the interface between enamel and the damage oral biofilm, which modulates the attachment of bacteria found in oral biofilm. The overall goal of this study was to gain insight into the biological formation of the human in vivo AEP. This study hypothesized that AEP is created by the formation of successive protein layers, which consist of initial binding to enamel and subsequent protein-protein interactions. This hypothesis was examined by observing quantitative and qualitative changes in pellicle composition during the first two hours of AEP formation in the oral cavity. Quantitative mass spectrometry approaches were used to generate an AEP protein profile for each time-point studied. Relative proteomic quantification was carried out for the 50 proteins observed in all four time-points. Notably, the abundance of important salivary proteins, such as histatin 1, decrease with increasing of the AEP formation, while other essential proteins such as statherin showed constant relative abundance in all time-points. In summary, this is the first study that investigates the dynamic process to the AEP formation by using proteomic approaches. Our data demonstrated that there are significant qualitative and quantitative proteome changes during the AEP formation, which in turn will likely impact the development of oral biofilms.
Highlights
The composition of the acquired enamel pellicle (AEP) formed in vivo has been studied by many techniques, including microscopy [1], amino acid analysis [2,3], gel-filtration and ion-exchange chromatography [4,5], and electrophoresis and immunoblotting [6,7,8,9,10,11,12]
We have successfully identified 130 AEP proteins, which have been characterized according to origin, putative biological function and possible role in AEP structure
For the proteome identification of the AEP, formed in all four different time-points carried out in this study, a total of 89 different proteins were identified in 5-min AEP formation, 92 different proteins were identified in 10-min AEP formation, 107 different proteins were identified in 60-min AEP formation and 101 different proteins were identified in 120-min AEP formation (Table 1)
Summary
The composition of the acquired enamel pellicle (AEP) formed in vivo has been studied by many techniques, including microscopy [1], amino acid analysis [2,3], gel-filtration and ion-exchange chromatography [4,5], and electrophoresis and immunoblotting [6,7,8,9,10,11,12]. All of these studies have been limited by the difficulties encountered in obtaining adequate amounts of AEP material for classical biochemical characterization [13]. The latter oral fluid contributor enters the oral cavity through the gingival crevice
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have