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Complementary structural information of positive- and negative-ion MSn spectra of glycopeptides with neutral and sialylated N-glycans.
Rapid Commun Mass Spectrom. 2006; 20(5):741-6.RC

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.

Authors+Show Affiliations

Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo 001-0021, Japan. deguchi@glyco.sci.hokudai.ac.jpNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16456804

Citation

Deguchi, Kisaburo, et al. "Complementary Structural Information of Positive- and Negative-ion MSn Spectra of Glycopeptides With Neutral and Sialylated N-glycans." Rapid Communications in Mass Spectrometry : RCM, vol. 20, no. 5, 2006, pp. 741-6.
Deguchi K, Ito H, Takegawa Y, et al. Complementary structural information of positive- and negative-ion MSn spectra of glycopeptides with neutral and sialylated N-glycans. Rapid Commun Mass Spectrom. 2006;20(5):741-6.
Deguchi, K., Ito, H., Takegawa, Y., Shinji, N., Nakagawa, H., & Nishimura, S. (2006). Complementary structural information of positive- and negative-ion MSn spectra of glycopeptides with neutral and sialylated N-glycans. Rapid Communications in Mass Spectrometry : RCM, 20(5), 741-6.
Deguchi K, et al. Complementary Structural Information of Positive- and Negative-ion MSn Spectra of Glycopeptides With Neutral and Sialylated N-glycans. Rapid Commun Mass Spectrom. 2006;20(5):741-6. PubMed PMID: 16456804.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Complementary structural information of positive- and negative-ion MSn spectra of glycopeptides with neutral and sialylated N-glycans. AU - Deguchi,Kisaburo, AU - Ito,Hiroki, AU - Takegawa,Yasuhiro, AU - Shinji,Nagai, AU - Nakagawa,Hiroaki, AU - Nishimura,Shin-Ichiro, PY - 2006/2/4/pubmed PY - 2006/4/7/medline PY - 2006/2/4/entrez SP - 741 EP - 6 JF - Rapid communications in mass spectrometry : RCM JO - Rapid Commun Mass Spectrom VL - 20 IS - 5 N2 - 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. SN - 0951-4198 UR - https://www.unboundmedicine.com/medline/citation/16456804/Complementary_structural_information_of_positive__and_negative_ion_MSn_spectra_of_glycopeptides_with_neutral_and_sialylated_N_glycans_ L2 - https://doi.org/10.1002/rcm.2368 DB - PRIME DP - Unbound Medicine ER -