Abstract
We aimed to comprehensively compare two compartmented oral proteomes, the salivary and the dental pellicle proteome. Systematic review and datamining was used to obtain the physico-chemical, structural, functional and interactional properties of 1,515 salivary and 60 identified pellicle proteins. Salivary and pellicle proteins did not differ significantly in their aliphatic index, hydrophaty, instability index, or isoelectric point. Pellicle proteins were significantly more charged at low and high pH and were significantly smaller (10–20 kDa) than salivary proteins. Protein structure and solvent accessible molecular surface did not differ significantly. Proteins of the pellicle were more phosphorylated and glycosylated than salivary proteins. Ion binding and enzymatic activities also differed significantly. Protein-protein-ligand interaction networks relied on few key proteins. The identified differences between salivary and pellicle proteins could guide proteome compartmentalization and result in specialized functionality. Key proteins could be potential targets for diagnostic or therapeutic application.
Highlights
We aimed to comprehensively compare two compartmented oral proteomes, the salivary and the dental pellicle proteome
The oral cavity comprises hundreds of proteins with a large range of biological functions like immune defense and biofilm homeostasis, nutrient decomposition and remineralization of dental hard tissues[1,2]. These proteins are characterized by molecular features, which are abstractly expressed by scores like aliphatic index, hydrophaty, instability index, net charge and isoelectric point
All proteins in the pellicle proteome were reported in the salivary proteome
Summary
We aimed to comprehensively compare two compartmented oral proteomes, the salivary and the dental pellicle proteome. The oral cavity comprises hundreds of proteins with a large range of biological functions like immune defense and biofilm homeostasis, nutrient decomposition and remineralization of dental hard tissues[1,2] These proteins are characterized by molecular features, which are abstractly expressed by scores like aliphatic index, hydrophaty, instability index, net charge and isoelectric point. To understand the organization and function of a proteome and to identify possible targets for medical diagnostics or therapy, the individual properties and the resulting relevance of a protein in a specific environment needs to be explored[4,5] Such deeper understanding of all proteins in a proteome would allow to identify possible physico-chemical, structural or functional patterns, which might facilitate a deeper comprehension of the local protein biology and aid translation of obtained findings to other proteomes[4,6]. Given that single studies are usually unable to allow full statistical exploration of a larger number of properties and suffer from limited reliability, a systematic review and datamining approach was taken
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