Chemical & Pharmaceutical Structure Analysis
Where Technology and Solutions Meet

CPSA 2011

Science and Technology Coming Together to Make a Difference

October 3 - 6, 2011
Bucks County Sheraton Hotel
Langhorne, PA


Poster Abstract #28

Automatic MS/MS characterization of N-linked Glycopeptides

Andrea Kiehne, Anja Resemann, Ulrike Schweiger-Hufnagel, Arndt Asperger, Detlev Suckau

Bruker Daltonik, Bremen, Germany

Glycosylation is the most abundant posttranslational protein modification. Involved in many relevant bio-logical processes and pathways, it is crucial to the understanding of many diseases. However, glyco-peptide analysis is still challenging. Due to high glycan heterogeneity and ion suppression effects, abundance of glycopeptides in tryptic digests is low and may require enrichment and separation tech-niques. In addition, interpretation of MS/MS spectra is difficult as classical database search approaches cannot be used when the peptide sequence and the glycan molecular weight are unknown. The proper determination of the peptide mass, i.e., the aglycone, is the key for automated glycan database searches. We developed a software approach evaluating the peptide mass in MALDI-TOF/TOF MS/MS and ESI LC-MS/MS spectra of N-linked glycopeptides.

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