Premium
MALDI‐TOF‐MS analysis of sialylated glycans and glycopeptides using 4‐chloro‐α‐cyanocinnamic acid matrix
Author(s) -
Selman Maurice H. J.,
Hoffmann Marcus,
Zauner Gerhild,
McDonnell Liam A.,
Balog Crina I. A.,
Rapp Erdmann,
Deelder André M.,
Wuhrer Manfred
Publication year - 2012
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201100498
Subject(s) - chemistry , glycan , chromatography , glycoproteomics , matrix assisted laser desorption/ionization , glycopeptide , matrix (chemical analysis) , mass spectrometry , biochemistry , glycoprotein , organic chemistry , adsorption , desorption , antibiotics
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.