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Friday

 

Study: Protein samples ready for mass spectrometry (MS): multiple reaction monitoring MS provides a reliable means to detect protein modification and may shed light on the cellular mechanisms behind chronic diseases

Recently, O-linked N-acetylglucosamine (O-GlcNAc), a sugar ring that reversibly modifies proteins inside the cell nucleus and cytoplasm in a process known as O-GlcNAcylation, has been revealed to be a key regulator of cell signaling in the body. Researchers believe that cellular changes induced by O-GlcNAc may be linked to chronic diseases, such as diabetes and cancer. Characterizing such dynamic relationships, however, is challenging.

Normally, O-GlcNAc detection relies on 'shotgun' mass spectrometry (MS), which breaks proteins into sequence-specific peptide chains and measures their molecular weight. But as O-GlcNAcylated peptides are present in such small amounts, building up concentrations sufficient for detection requires time-consuming and tedious enrichment methods.

Now, Julien Maury and Andre Choo from the A*STAR Bioprocessing Technology Institute in Singapore and co-workers have developed a simple way to detect native O-GlcNAcylated proteins—even at 10,000-fold dilution—with a targeted MS technique known as multiple reaction monitoring (MRM).

Instead of scrutinizing all possible peptides from a protein system, MRM-MS filters out masses that correspond to an expected precursor ion. Then, the joined-up precursor peptide and selected fragment ions—termed 'transition couples'—are monitored to build up a quantitative assay of the protein structure.
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