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Complementary structural information of positive- and negative-ion MSn spectra of glycopeptides with neutral and sialylated N-glycans
| 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)
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Submitter: 出口 喜三郎
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