C60-fullerene bound silica for the preconcentration and the fractionation of multiphosphorylated peptides |
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Authors: | Martin Fischnaller Rania Bakry Rainer M Vallant Lukas A Huber Günther K Bonn |
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Institution: | 1. Institute of Analytical Chemistry and Radiochemistry, Leopold Franzens University, Innrain 80-82, 6020 Innsbruck, Austria;2. Biocenter, Division of Cell Biology, Innsbruck Medical University, Innrain 80-82, 6020 Innsbruck, Austria |
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Abstract: | Phosphorylation of proteins is an important cellular regulatory process. The analysis of protein phosphorylation is challenging due to the high dynamic range and low abundance natures of phosphorylated species. Mass spectrometry (MS) of phosphopeptides obtained from tryptic protein digests is the method-of-choice for characterization of phosphorylated proteins. However, determination of phosphopeptides by MS represents a major challenge, especially in the presence of unmodified peptides. Due to lower ionization efficiency of phosphopeptides, as well as the fact that the stoichiometry of phosphorylation is often present at low relative abundance, efficient enrichment of the phosphorylated peptides prior to MS analysis is therefore of high demand. In addition, successful identification of peptides with different phosphorylation grades still remains challenging. |
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Keywords: | C60-fullerene Phosphopeptides Grade of phosphorylation MALDI-MS Enrichment Sample preparation |
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