Oral Sessions
- Day 3, May 13（Wed.） 14:30-14:50 Room B (1202)
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3B-O14-1430 PDF
Analysis of the primary structure of proteins by trapped-ion mobility mass spectrometry
The main component of biologics represented in therapeutic antibodies is a protein. Their activities are affected by post-translational modifications in their primary structure such as glycosylation, deamidation, and oxidation, etc. Peptide mapping with mass spectrometry can determine the location, type, and quantity of the modification from the accurate masses of proteolytic digests (generally tryptic) of the target protein. In the case of protein samples, the amount of sample obtained is often low, so high-sensitive machines and methods are significant. Trapped-ion mobility mass spectrometry can separate molecules by their ion mobility (reflect molecular shape) and m/z, so the overlap of signal peaks is less than that of conventional mass spectrometry. Therefore even the poor signal peptides can be identified, so the higher sequence coverage can be expected even if in the case of low amount samples. In this presentation, the analysis of the primary structure of proteins by trapped-ion mobility mass spectrometry will be discussed.