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Direct structural assignment of neutral and sialylated N-glycans of glycopeptides using collision-induced dissociation MSⁿ spectral matching.
| Title: | Direct structural assignment of neutral and sialylated N-glycans of glycopeptides using collision-induced dissociation MSⁿ spectral matching. |
| Authors: | Ito, Hiroki Browse this author | | Takegawa, Yasuhiro Browse this author | | Deguchi, Kisaburo Browse this author | | Nagai, Shinji Browse this author | | Nakagawa, Hiroaki Browse this author | | Shinohara, Yasuro Browse this author | | Nishimura, Shin-Ichiro Browse this author →KAKEN DB |
| Issue Date: | 2006 |
| Journal Title: | Rapid Communications in Mass Spectrometry |
| Volume: | 20 |
| Issue: | 23 |
| Start Page: | 3557 |
| End Page: | 3565 |
| Publisher DOI: | 10.1002/rcm.2761 |
| PMID: | 17091533 |
| Abstract: | Mass spectrometric analyses of various N-glycans binding to proteins and peptides are highly desirable for elucidating their biological roles. An approach based on collision-induced dissociation (CID) MSⁿ spectra acquired by electrospray ionization linear ion trap time-of-flight mass spectrometry (ESI-LIT-TOFMS) in the positive- and negative-ion modes has been proposed as a direct method of assigning N-glycans without releasing them from N-glycopeptides. In the positive-ion mode of this approach, the MS² spectrum of N-glycopeptide was acquired so that a glycoside-bond cleavage occurs in the chitobiose residue (i.e., GlcNAcβ1-4GlcNAc, GlcNAc: N-acetylglucosamine) attached to asparagine (N), and two charges on the [M+H+Na]²+ precursor ion are shared with both of the resulting fragments. These fragments are sodiated Bn-type fragment ions of oligosaccharide (N-glycan) and a protonated peptide ion retaining one GlcNAc residue on the asparagine (N) residue. The structure of N-glycan was assigned by comparing MS³ spectra derived from both the sodiated Bn-type fragment ions of N-glycopeptide and the PA (2-aminopyridine) N-glycan standard (i.e., MSⁿ spectral matching). In a similar manner, the structural assignment of sialylated N-glycan was performed by employing the negative-ion CID MSⁿ spectra of deprotonated Bn-type fragment ions of N-glycopeptide and the PA N-glycan standard. The efficacy of this approach was tested with chicken egg yolk glycopeptides with a neutral and a sialylated N-glycan, and human serum IgG glycopeptides with neutral N-glycan isomers. These results suggest that the approach based on MSⁿ spectral matching is useful for the direct and simple structural assignment of neutral and sialylated N-glycans of glycopeptides. Copyright © 2006 John Wiley & Sons, Ltd. |
| Rights: | Copyright © 2006 John Wiley & Sons, Inc., Rapid Communications in Mass Spectrometry, 20(23)3557-3565 |
| Relation: | http://www.interscience.wiley.com/ | | http://www3.interscience.wiley.com/cgi-bin/jhome/4849 |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/17086 |
| 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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