Mass spectrometry for Palaeoprotemics

MASS SPECTROMETRY FOR PALAEOPROTEOMICS

The latest generation of high-resolution tandem mass spectrometry for palaeoproteomics can reliably and rapidly detect proteins in complex mixtures, even in the very limited quantities typical of ancient samples. Workflow miniaturization and simplification of sample preparation, by integrating into a single or few step(s) different chemical treatments, have already been proven to improve recovery in the most recalcitrant ancient samples. Such approaches are contributing to minimizing the amount of starting material needed for palaeoproteomics analysis. The possibility to combine the dissociative capabilities of complementary fragmentation methods (ETD, UVPD, HCD) maximises the ability to elucidate the full complexity of the protein material, in sequence, in polymorphism and in chemical and/or post-translational modifications with unprecedented depth and accuracy. Top-down methods, adding molecular details lost when proteoforms are hydrolyzed into proteolytic peptides in bottom-up proteomics, also benefit from the recent technological gains in mass spectrometry. The ESR10 will develop new minimally invasive methods and miniaturized analytical workflow based on bottom-up and top-down approaches, to analyse trace level of proteins in palaeoanthropological and palaeontological materials and reach an exhaustive characterization of ancient material available. Digestion free top-down proteomics methods will also be investigated to remove many of the limitations hampering analysis of this category of samples. The methods will be used to identify proteins from samples with very limited amounts. Elucidation of protein polymorphism will also be studied with these minimally invasive methods in partnership with the PUSHH partners. Another application of these methods is the study protein degradation (e.g. chemical modifications, breakdown) such as the degradation of tooth enamel proteins in partnership with ESR14.