Distinguishing N-acetylneuraminic acid linkage isomers on glycopeptides by ion mobility-mass spectrometry

Hinneburg, Hannes; Hofmann, Johanna; Struwe, Weston B.; Thader, A.; Altmann, Friedrich; Silva, D. Varón; Seeberger, Peter H.; Pagel, Kevin; Kolarich, Daniel

doi:10.1039/c6cc01114d

Cited by 88 publications

(113 citation statements)

References 28 publications

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“…Here, we report that the addition of IMS to conventional glycoproteomics platforms adds the ability to differentiate sialic acid linkage isomers on both N- and O-linked glycopeptides. During the revision stage of this article, another group reported a very similar strategy for differentiating sialylation linkage by IMS, 43 further illustrating the utility of this approach. With further optimization of separation conditions for closely related glycans present on biologically relevant glycan structures, IMS has the potential to extract a higher level of information from glycoproteomics.…”

Section: Resultsmentioning

confidence: 93%

Site-Specific Mapping of Sialic Acid Linkage Isomers by Ion Mobility Spectrometry

Guttman

Lee

2016

Anal. Chem.

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Detailed structural elucidation of protein glycosylation is a tedious process often involving several techniques. Glycomics and glycoproteomics approaches with mass spectrometry offer a rapid platform for glycan profiling but are limited by the inability to resolve isobaric species such as linkage and positional isomers. Recently, ion mobility spectrometry (IMS) has been shown to effectively resolve isobaric oligosaccharides, but the utility of IMS to obtain glycan structural information on a site-specific level with proteomic analyses has yet to be investigated. Here, we report that the addition of IMS to conventional glycoproteomics platforms adds additional information regarding glycan structure and is particularly useful for differentiation of sialic acid linkage isomers on both N- and O-linked glycopeptides. With further development IMS may hold the potential for rapid and complete structural elucidation of glycan chains at a site-specific level.

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Section: Resultsmentioning

confidence: 93%

Site-Specific Mapping of Sialic Acid Linkage Isomers by Ion Mobility Spectrometry

Guttman

Lee

2016

Anal. Chem.

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“…In IM-MS ions are separated in the gas-phase based on their mobilities (size/shape) as well as mass-to-charge ( m/z ). While IM-MS results have been demonstrated for rapid glycan separations, conventional approaches still suffer from limited sensitivity and resolution for analyses of isomeric glycoforms 2 , 7 , limiting their potential for broader utility. Metal adduction 8 , and use of other ligands 9 , have seen some effectiveness in increasing IM glycan resolution, but these approaches are still unable to resolve all isomeric glycoforms of interest.…”

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confidence: 99%

Unraveling the isomeric heterogeneity of glycans: ion mobility separations in structures for lossless ion manipulations

et al. 2018

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To address the challenges associated with glycan analyses, we have implemented a structures for lossless ion manipulations (SLIM) serpentine ultra-long path with extended routing (SUPER) ion mobility-mass spectrometry (i.e. SLIM SUPER IM-MS) platform to achieve much higher resolution of isomeric glycoforms. We have demonstrated the potential of this platform as a future component of the glycomics toolbox.

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“…The analysis of IM-MS can reveal information about the macro- and micro- heterogeneity of glycosylation of glycoconjugates. For example, IM can separate intact glycopeptides that differ only in the glycosylation sites [16]. Furthermore, IM-MS analysis of glycopeptide fragments was demonstrated to be an effective strategy to distinguish α2,3 versus α2,6 sialic acid linkages on intact glycopeptides [15,16].…”

Section: Improved Characterization Of Intact Glycoconjugatesmentioning

confidence: 99%

“…For example, IM can separate intact glycopeptides that differ only in the glycosylation sites [16]. Furthermore, IM-MS analysis of glycopeptide fragments was demonstrated to be an effective strategy to distinguish α2,3 versus α2,6 sialic acid linkages on intact glycopeptides [15,16]. In addition to glycopeptides, IM-MS was recently used to separate glycolipid isomers [57].…”

Section: Improved Characterization Of Intact Glycoconjugatesmentioning

confidence: 99%

Recent advances in ion mobility–mass spectrometry for improved structural characterization of glycans and glycoconjugates

Chen

Glover

2018

Current Opinion in Chemical Biology

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Glycans and glycoconjugates are involved in regulating a vast array of cellular and molecular processes. Despite the importance of glycans in biology and disease, characterization of glycans remains difficult due to their structural complexity and diversity. Mass spectrometry (MS)-based techniques have emerged as the premier analytical tools for characterizing glycans. However, traditional MS-based strategies struggle to distinguish the large number of coexisting isomeric glycans that are indistinguishable by mass alone. Because of this, ion mobility spectrometry coupled to MS (IM-MS) has received considerable attention as an analytical tool for improving glycan characterization due to the capability of IM to resolve isomeric glycans before MS measurements. In this review, we present recent improvements in IM-MS instrumentation and methods for the structural characterization of isomeric glycans. In addition, we highlight recent applications of IM-MS that illustrate the enormous potential of this technology in a variety of research areas, including glycomics, glycoproteomics, and glycobiology.

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Distinguishing N-acetylneuraminic acid linkage isomers on glycopeptides by ion mobility-mass spectrometry

Cited by 88 publications

References 28 publications

Site-Specific Mapping of Sialic Acid Linkage Isomers by Ion Mobility Spectrometry

Site-Specific Mapping of Sialic Acid Linkage Isomers by Ion Mobility Spectrometry

Unraveling the isomeric heterogeneity of glycans: ion mobility separations in structures for lossless ion manipulations

Recent advances in ion mobility–mass spectrometry for improved structural characterization of glycans and glycoconjugates

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