Ultra-high resolution top down Fourier-transform mass spectrometry experiments reveal microheterogeneity of human salivary proteins.

摘要

Complementary to bottom-up approaches, top-down proteomics is being applied as a powerful method to provide complete characterization of protein primary structure of proteins. The strength of this method lies in its capacity to provide an unprejudiced description of genetic sequence polymorphism and post-translational modifications. Amongst all types of proteomics studies, the analysis of biological fluids such as saliva offers particular advantages including their availability and their non invasive collection. In our study this biological fluid is investigated as a potential source of disease biomarkers and therapeutic targets. To this view the description of protein isoforms, and intra- and inter- individual polymorphisms would provide a better understanding of structure/function relationships of proteins and the discovery of disease biomarkers.