Journal
PROTEOMICS
Volume 12, Issue 9, Pages 1337-1348Publisher
WILEY
DOI: 10.1002/pmic.201100498
Keywords
Antibody; Glycoproteomics; Glycosylation; Mass spectrometry; Matrix; Posttranslational modification
Funding
- Hoffmann la Roche
Ask authors/readers for more resources
For MALDI analysis of glycans and glycopeptides, the choice of matrix is crucial inminimizing desialylation by mass spectrometric in-source and metastable decay. Here, we evaluated the potential of 4-chloro-alpha-cyanocinnamic acid (Cl-CCA) for MALDI-TOF-MS analysis of labile sialylated tryptic N-glycopeptides and released N- and O-glycans. Similar to DHB, but in contrast to CHCA, the Cl-CCA matrix allowed the analysis of sialylated N-glycans and glycopeptides in negative ion mode MALDI-TOF-MS. Dried droplet preparations of Cl-CCA provided microcrystals with a homogeneous spatial distribution and high shot-to-shot repeatability similar to CHCA, which simplified the automatic measurement and improved the resolution and mass accuracy. Interestingly, reflectron-positive ion mode analysis of 1-phenyl-3-methyl-5-pyrazolone (PMP)-labeled O-glycans with Cl-CCA revealed more complete profiles than with DHB and CHCA. In conclusion, we clearly demonstrate the high potential of this rationally designed matrix for glycomics and glycoproteomics.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available