Engaging challenges in glycoproteomics: Recent advances in MS-based glycopeptide analysis

Venkata Kolli, Katherine N. Schumacher, Eric D. Dodds

Research output: Contribution to journalReview article

31 Citations (Scopus)

Abstract

The proteomic analysis of glycosylation is uniquely challenging. The numerous and varied biological roles of protein-linked glycans have fueled a tremendous demand for technologies that enable rapid, in-depth structural examination of glycosylated proteins in complex biological systems. In turn, this demand has driven many innovations in wide ranging fields of bioanalytical science. This review will summarize key developments in glycoprotein separation and enrichment, glycoprotein proteolysis strategies, glycopeptide separation and enrichment, the role of mass measurement accuracy in glycopeptide detection, glycopeptide ion dissociation methods for MS/MS, and informatic tools for glycoproteomic analysis. In aggregate, this selection of topics serves to encapsulate the present status of MS-based analytical technologies for engaging the challenges of glycoproteomic analysis.

Original languageEnglish (US)
Pages (from-to)113-131
Number of pages19
JournalBioanalysis
Volume7
Issue number1
DOIs
StatePublished - Jan 1 2015

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Glycopeptides
Glycoproteins
Proteolysis
Technology
Glycosylation
Informatics
Biological systems
Proteomics
Polysaccharides
Proteins
Innovation
Ions

ASJC Scopus subject areas

  • Analytical Chemistry
  • Pharmacology, Toxicology and Pharmaceutics(all)
  • Clinical Biochemistry
  • Medical Laboratory Technology

Cite this

Engaging challenges in glycoproteomics : Recent advances in MS-based glycopeptide analysis. / Kolli, Venkata; Schumacher, Katherine N.; Dodds, Eric D.

In: Bioanalysis, Vol. 7, No. 1, 01.01.2015, p. 113-131.

Research output: Contribution to journalReview article

Kolli, Venkata ; Schumacher, Katherine N. ; Dodds, Eric D. / Engaging challenges in glycoproteomics : Recent advances in MS-based glycopeptide analysis. In: Bioanalysis. 2015 ; Vol. 7, No. 1. pp. 113-131.
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