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Direct determination of glycosylation sites in O‐fucosylated glycopeptides using nano‐electrospray quadrupole time‐of‐flight mass spectrometry
Author(s) -
Maček Boris,
Hofsteenge Jan,
PeterKatalinić Jasna
Publication year - 2001
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.298
Subject(s) - chemistry , glycosylation , mass spectrometry , fucosylation , glycan , glycopeptide , electrospray , peptide , n linked glycosylation , chromatography , biochemistry , glycoprotein , antibiotics
O‐Fucosylation is an unusual posttranslational modification present in several proteins that play important roles in physiological processes such as coagulation, cell signaling and metastasis. Although the exact function of the modification is still unclear, the number of proteins found to be modified is increasing, and there is a need for further structural and functional analyses. Here we report on a rapid and straightforward approach in the analysis of glycosylation status and determination of glycosylation sites in O‐fucosylated glycopeptides using nano‐electrospray quadrupole time‐of‐flight (nano‐ESI Q‐TOF) mass spectrometry. In a single measurement of previously chemically untreated O‐fucosylated peptides originating from the thrombospondin‐1 repeats, we were able to determine the glycosylation status of the analyzed peptide, the glycosylation site, and the glycan structure. The abundance of glycosylated peptide fragment ions in MS 2 spectra suggests that nano‐ESI Q‐TOF mass spectrometry can be used as a general approach in structural studies of O‐fucosylation in proteins. Copyright © 2001 John Wiley & Sons, Ltd.