Titanium dioxide enrichment of sialic acid-containing glycopeptides

Giuseppe Palmisano, Sara Eun Lendal, Martin R. Larsen

Research output: Chapter in Book/Report/Conference proceedingChapter

22 Citations (Scopus)


Glycosylation is one of the many post-translational protein modifications that regulate several biological processes of proteins and lipids. In particular aberrant sialylation, at the terminal position of the glycan structures of cell surface proteins, occurs in numerous diseases such as cancer metastasis and viral infections. Methodological improvements in the sample preparation and analysis currently enable the detailed identification of the glycosylation sites and glycan structure characterization. In this context, the aim of this chapter is to describe a methodology to identify the glycosylation site of N-linked sialylated glycoproteins. The method relies on the specificity of titanium dioxide affinity chromatography to isolate sialic acid-containing glycopeptides. After enzymatic release of the glycans, the enriched sialylated glycopeptides are analyzed by mass spectrometry. This strategy was applied to a crude membrane fraction of EGF-stimulated HeLa cells metabolically labeled with SILAC enabling both qualitative and quantitative analyses of sialoglycopeptides.

Original languageEnglish
Title of host publicationGel-Free Proteomics
Subtitle of host publicationMethods and Protocols
Number of pages14
Publication statusPublished - 1 Dec 2011
Externally publishedYes

Publication series

NameMethods in Molecular Biology
ISSN (Print)1064-3745



  • Glycosylation
  • Mass spectrometry
  • Quantitative proteomics
  • Sialylation
  • Titanium dioxide

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

Cite this

Palmisano, G., Lendal, S. E., & Larsen, M. R. (2011). Titanium dioxide enrichment of sialic acid-containing glycopeptides. In Gel-Free Proteomics: Methods and Protocols (pp. 309-322). (Methods in Molecular Biology; Vol. 753). https://doi.org/10.1007/978-1-61779-148-2_21