Automated measurement of permethylated serum N-glycans by MALDI-linear ion trap mass spectrometry

Maïlys Guillard, Jolein Gloerich, Hans J.C.T. Wessels, Eva Morava, Ron A. Wevers, Dirk J. Lefeber

Research output: Contribution to journalArticlepeer-review

29 Scopus citations

Abstract

The use of N-glycan mass spectrometry for clinical diagnostics requires the development of robust high-throughput profiling methods. Still, structural assignment of glycans requires additional information such as MS2 fragmentation or exoglycosidase digestions. We present a setting which combines a MALDI ionization source with a linear ion trap analyzer. This instrumentation allows automated measurement of samples thanks to the crystal positioning system, combined with MSn sequencing options. 2,5-Dihydroxybenzoic acid, commonly used for the analysis of glycans, failed to produce the required reproducibility due to its non-homogeneous crystallization properties. In contrast, α-cyano-4-hydroxycinnamic acid provided a homogeneous crystallization pattern and reproducibility of the measurements. Using serum N-glycans as a test sample, we focused on the automation of data collection by optimizing the instrument settings. Glycan structures were confirmed by MS2 analysis. Although sample processing still needs optimization, this method provides a reproducible and high-throughput approach for measurement of N-glycans using a MALDI-linear ion trap instrument.

Original languageEnglish (US)
Pages (from-to)1550-1557
Number of pages8
JournalCarbohydrate Research
Volume344
Issue number12
DOIs
StatePublished - Aug 17 2009

Keywords

  • Glycan profiling
  • Glycosylation
  • Linear ion trap
  • MALDI
  • N-glycans
  • α-Cyano-4-hydroxycinnamic acid

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Organic Chemistry

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