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Complementary structural information of positive- and negative-ion MSn spectra of glycopeptides with neutral and sialylated N-glycans

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Title: Complementary structural information of positive- and negative-ion MSn spectra of glycopeptides with neutral and sialylated N-glycans
Authors: Deguchi, Kisaburo1 Browse this author
Ito, Hiroki Browse this author
Takegawa, Yasuhiro Browse this author →KAKEN DB
Shinji, Nagai Browse this author
Nakagawa, Hiroaki Browse this author
Nishimura, Shin-Ichiro Browse this author →KAKEN DB
Authors(alt): 出口, 喜三郎1
Issue Date: 2006
Publisher: John Wiley & Sons
Journal Title: Rapid Communications in Mass Spectrometry
Volume: 20
Issue: 5
Start Page: 741
End Page: 746
Publisher DOI: 10.1002/rcm.2368
PMID: 16456804
Abstract: Positive- and negative-ion MSn spectra of chicken egg yolk glycopeptides binding a neutral and a sialylated N-glycan were acquired by using electrospray ionization linear ion trap time-of-flight mass spectrometry (ESI-LIT-TOFMS) and collision-induced dissociation (CID) with helium as collision gas. Several characteristic differences were observed between the positive- and negative-ion CID MSn (n = 2, 3) spectra. In the positive-ion MS2 spectra, the peptide moiety was presumably stable, but the neutral N-glycan moiety caused several B-type fragmentations and the sialylated N-glycan almost lost sialic acid(s). In contrast, in the negative-ion MS2 spectra, the peptide moiety caused several side-chain and N-glycan residue (e.g., N-acetylglucosamine (GlcNAc) residue) fragmentations in addition to backbone cleavages, but the N-glycan moieties were relatively stable. The positive-ion MS3 spectra derived from the protonated peptide ion containing a GlcNAc residue (203.1 Da) provided enough information to determine the peptide amino-acid sequence including the glycosylation site, while the negative-ion MS3 spectra derived from the deprotonated peptide containing a 0,2X1-type cross-ring cleavage (83.1 Da) complicated the peptide sequence analysis due to side-chain and 0,2X1 residue related fragmentations. However, for the structural information of the N-glycan moiety of the glycopeptides, the negative-ion CID MS3 spectra derived from the deprotonated 2,4A6-type cross-ring cleavage ion (neutral N-glycan) or the doubly deprotonated B6-type fragment ion (sialylated N-glycan) are more informative than are those of the corresponding positive-ion CID MS3 spectra. Thus, the positive-ion mode of CID is useful for the analyses of peptide amino-acid sequences including the glycosylation site. The negative-ion mode of CID is especially useful for sialylated N-glycan structural analysis. Therefore, in the structural analysis of N-glycopeptides, their roles are complementary.
Rights: Copyright © 2006 John Wiley & Sons, Inc., Rapid Communications in Mass Spectrometry, 20(5), p741-746
Relation: http://www.interscience.wiley.com/
Type: article (author version)
URI: http://hdl.handle.net/2115/6112
Appears in Collections:理学院・理学研究院 (Graduate School of Science / Faculty of Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 出口 喜三郎

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