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Direct structural assignment of neutral and sialylated N-glycans of glycopeptides using collision-induced dissociation MSⁿ spectral matching.

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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)

Submitter: 出口 喜三郎

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