Abstract
Studies on small quantity, highly complex protein samples, such as salivary pellicle, have been enabled by recent major technological and analytical breakthroughs. Advances in mass spectrometry-based computational proteomics such as Multidimensional Protein Identification Technology have allowed precise identification and quantification of complex protein samples on a proteome-wide scale, which has enabled the determination of corresponding genes and cellular functions at the protein level. The latter was achieved via protein-protein interaction mapping with Gene Ontology annotation. In recent years, the application of these technologies has broken various barriers in small-quantity-complex-protein research such as salivary pellicle. This review provides a concise summary of contemporary proteomic techniques contributing to (1) increased complex protein (up to hundreds) identification using minute sample sizes (µg level), (2) precise protein quantification by advanced stable isotope labelling or label-free approaches and (3) the emerging concepts and techniques regarding computational integration, such as the Gene Ontology Consortium and protein-protein interaction mapping. The latter integrates the structural, genomic, and biological context of proteins and genes to predict protein interactions and functional connections in a given biological context. The same technological breakthroughs and computational integration concepts can also be applied to other low-volume oral protein complexes such as gingival crevicular or peri-implant sulcular fluids.
Highlights
Often, due to a lack of suitable experimental protocols, and small quantities of highly complex protein samples acquired from the oral cavity, such as salivary pellicle, limits the information that can be extracted from such samples
As the oral cavity is a unique portal where mineralized tissue is directly exposed to heavy colonization of oral microbiota, it is plausible that the acquired salivary pellicle interfacing between tooth surfaces, the oral environment, and intimate contacts with oral microbes could hold essential biological functions, such as protection from demineralization, buffering bacterial acids or other toxic by-products that may lead to dental caries initiation [8]
Salivary pellicle proteins exist in small amounts [15], removing the attached proteins from specimen surfaces without contamination is crucial for accurate analysis
Summary
Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations. Known as acquired enamel pellicle, is an important interface structure/proteinaceous material located between dental hard tissue surfaces and the oral environment which modulates the biological and microbiological activities on tooth surfaces [2]. Often, due to a lack of suitable experimental protocols, and small quantities of highly complex protein samples acquired from the oral cavity, such as salivary pellicle, limits the information that can be extracted from such samples. As the oral cavity is a unique portal where mineralized tissue is directly exposed to heavy colonization of oral microbiota, it is plausible that the acquired salivary pellicle interfacing between tooth surfaces, the oral environment, and intimate contacts with oral microbes could hold essential biological functions, such as protection from demineralization, buffering bacterial acids or other toxic by-products that may lead to dental caries initiation [8]. The scientific approaches in understanding salivary pellicle proteins on tooth surfaces are of great importance in comprehending their roles and relationships with oral microbes and dental disease pathogenesis
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