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Structural assignment of isomeric 2-aminopyridine-derivatized monosialylated biantennary N-linked oligosaccharides using negative-ion multistage tandem mass spectral matching.
Rapid Commun Mass Spectrom. 2006; 20(3):412-8.RC

Abstract

To investigate the possibility of structural assignment based on negative-ion tandem multistage (MSn) mass spectral matching, four isomers of 2-aminopyridine (PA)-derivatized monosialylated oligosaccharides (i.e., complex-type N-glycans with an alpha2-3- or alpha2-6-linked sialic acid on alpha1-6 or alpha1-3 antennae) were analyzed using high-performance liquid chromatography/electrospray ion trap time-of-flight mass spectrometry (HPLC/ESI-IT-TOFMS). The negative ion [M-2H]2- is observed predominantly in the MS1 spectra without the loss of a sialic acid. The MS2 spectra derived from it are sufficiently reproducible that MS2 spectral matching based on correlation coefficients can be applied to the assignment of these isomers. The isomers containing a sialic acid on alpha1-6 or alpha1-3 antennae can be distinguished by MS2 spectral matching, but the alpha2-3 and alpha2-6 linkage types of sialic acid cannot be distinguished by their MS2 spectra. However, MS3 spectra derived from fragment ions containing a sialic acid (i.e., C4- and D-type ions) clearly differentiate the alpha2-3 and alpha2-6 linkage types of sialic acid in their MS3 spectral patterns. This difference might be rationalized in terms of a proton transfer from the reducing-end mannose to the negatively charged sialic acid. These two moieties are very close in the structural conformations of the precursor C4-type fragment ions of alpha2-6 linkage type, as predicted by molecular mechanics calculations. Thus, negative-ion MSn (n = 2, 3) spectral matching was demonstrated to be useful for the structural assignment of these four monosialylated PA N-glycan isomers.

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 availableNo affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

16381065

Citation

Deguchi, Kisaburo, et al. "Structural Assignment of Isomeric 2-aminopyridine-derivatized Monosialylated Biantennary N-linked Oligosaccharides Using Negative-ion Multistage Tandem Mass Spectral Matching." Rapid Communications in Mass Spectrometry : RCM, vol. 20, no. 3, 2006, pp. 412-8.
Deguchi K, Takegawa Y, Ito H, et al. Structural assignment of isomeric 2-aminopyridine-derivatized monosialylated biantennary N-linked oligosaccharides using negative-ion multistage tandem mass spectral matching. Rapid Commun Mass Spectrom. 2006;20(3):412-8.
Deguchi, K., Takegawa, Y., Ito, H., Miura, N., Yoshioka, S., Nagai, S., Nakagawa, H., & Nishimura, S. (2006). Structural assignment of isomeric 2-aminopyridine-derivatized monosialylated biantennary N-linked oligosaccharides using negative-ion multistage tandem mass spectral matching. Rapid Communications in Mass Spectrometry : RCM, 20(3), 412-8.
Deguchi K, et al. Structural Assignment of Isomeric 2-aminopyridine-derivatized Monosialylated Biantennary N-linked Oligosaccharides Using Negative-ion Multistage Tandem Mass Spectral Matching. Rapid Commun Mass Spectrom. 2006;20(3):412-8. PubMed PMID: 16381065.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structural assignment of isomeric 2-aminopyridine-derivatized monosialylated biantennary N-linked oligosaccharides using negative-ion multistage tandem mass spectral matching. AU - Deguchi,Kisaburo, AU - Takegawa,Yasuhiro, AU - Ito,Hiroki, AU - Miura,Nobuaki, AU - Yoshioka,Shinji, AU - Nagai,Shinji, AU - Nakagawa,Hiroaki, AU - Nishimura,Shin-Ichiro, PY - 2005/12/29/pubmed PY - 2006/3/24/medline PY - 2005/12/29/entrez SP - 412 EP - 8 JF - Rapid communications in mass spectrometry : RCM JO - Rapid Commun Mass Spectrom VL - 20 IS - 3 N2 - To investigate the possibility of structural assignment based on negative-ion tandem multistage (MSn) mass spectral matching, four isomers of 2-aminopyridine (PA)-derivatized monosialylated oligosaccharides (i.e., complex-type N-glycans with an alpha2-3- or alpha2-6-linked sialic acid on alpha1-6 or alpha1-3 antennae) were analyzed using high-performance liquid chromatography/electrospray ion trap time-of-flight mass spectrometry (HPLC/ESI-IT-TOFMS). The negative ion [M-2H]2- is observed predominantly in the MS1 spectra without the loss of a sialic acid. The MS2 spectra derived from it are sufficiently reproducible that MS2 spectral matching based on correlation coefficients can be applied to the assignment of these isomers. The isomers containing a sialic acid on alpha1-6 or alpha1-3 antennae can be distinguished by MS2 spectral matching, but the alpha2-3 and alpha2-6 linkage types of sialic acid cannot be distinguished by their MS2 spectra. However, MS3 spectra derived from fragment ions containing a sialic acid (i.e., C4- and D-type ions) clearly differentiate the alpha2-3 and alpha2-6 linkage types of sialic acid in their MS3 spectral patterns. This difference might be rationalized in terms of a proton transfer from the reducing-end mannose to the negatively charged sialic acid. These two moieties are very close in the structural conformations of the precursor C4-type fragment ions of alpha2-6 linkage type, as predicted by molecular mechanics calculations. Thus, negative-ion MSn (n = 2, 3) spectral matching was demonstrated to be useful for the structural assignment of these four monosialylated PA N-glycan isomers. SN - 0951-4198 UR - https://www.unboundmedicine.com/medline/citation/16381065/Structural_assignment_of_isomeric_2_aminopyridine_derivatized_monosialylated_biantennary_N_linked_oligosaccharides_using_negative_ion_multistage_tandem_mass_spectral_matching_ DB - PRIME DP - Unbound Medicine ER -