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MALDI-TOF-MS Analysis of Sialylated Glycans and Glycopeptides Using 4-chloro-α-cyanocinnamic Acid Matrix

MALDI-TOF-MS Analysis of Sialylated Glycans and Glycopeptides Using 4-chloro-α-cyanocinnamic Acid Matrix

Maurice H J Selman, Marcus Hoffmann, Gerhild Zauner, Liam A McDonnell, Crina I A Balog, Erdmann Rapp, André M Deelder, Manfred Wuhrer

Proteomics. 2012 May;12(9):1337-48.

PMID: 22589184

Abstract:

For MALDI analysis of glycans and glycopeptides, the choice of matrix is crucial in minimizing desialylation by mass spectrometric in-source and metastable decay. Here, we evaluated the potential of 4-chloro-α-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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP69727077	4-Chloro-α-cyanocinnamic acid		69727-07-7	Price

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