“Ghost” Fragment Ions in Structure and Site-Specific Glycoproteomics Analysis
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Le résumé fourni par la source
Mass spectrometry (MS) can unlock crucial insights into the intricate world of glycosylation analysis. Despite its immense potential, the qualitative and quantitative analysis of isobaric glycopeptide structures remains one of the most daunting hurdles in the field of glycoproteomics. The ability to distinguish between these complex glycan structures poses a significant challenge, hindering our ability to accurately measure and understand the role of glycoproteins in biological systems. A few recent publications described the use of collision energy (CE) modulation to improve structural elucidation, especially for qualitative purposes. Different linkages of glycan units usually demonstrate different stabilities under CID/HCD fragmentation conditions. Fragmentation of the glycan moiety produces low molecular weight ions (oxonium ions) that can serve as a structure-specific signature for specific glycan moieties; however, the specificity of these fragments has never been examined closely. Here, we particularly focused on N-glycoproteomics analysis and investigated fragmentation specificity using synthetic stable isotope-labeled N-glycopeptide standards. These standards were isotopically labeled at the reducing terminal GlcNAc, which allowed us to resolve fragments produced by the oligomannose core moiety and fragments generated from outer antennary structures. Our research identified the potential for false-positive structure assignments due to the occurrence of "Ghost" fragments resulting from single glyco unit rearrangement or mannose core fragmentation within the collision cell. To mitigate this issue, we have established a minimal intensity threshold for these fragments to prevent misidentification of structure-specific fragments in glycoproteomics analysis. Our findings provide a crucial step forward in the quest for more accurate and reliable glycoproteomics measurements.
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Le contrôle bibliographique ouvert
DOI retrouvé dans Crossref DOI retrouvé ; titre concordant.
- Titre Crossref
- “Ghost” Fragment Ions in Structure and Site-Specific Glycoproteomics Analysis
- Date Crossref
- 29/06/2023
- Éditeur
- American Chemical Society (ACS)
- Type
- journal-article
Ce recoupement confirme des métadonnées liées au DOI. Il ne confirme ni la méthode ni les conclusions de l’étude, et il ne compte pas comme une seconde source scientifique indépendante.
Où se fait cette recherche
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Max Planck Institute for Heart and Lung Research pays non établi dans la noticeStructure de recherche
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George Mason University pays non établi dans la noticeUniversité ou école supérieure
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University of Maryland Department of Chemistry and Biochemistry pays non établi dans la noticeUniversité ou école supérieure
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Georgetown University Clinical and Translational Glycoscience Research Center pays non établi dans la noticeUniversité ou école supérieure
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Georgetown University Medical Center pays non établi dans la noticeÉtablissement de santé
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Max-Planck-Institut fuer Herz- und Lungenforschung pays non établi dans la noticeStructure de recherche
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College of Engineering and Computing Department of Bioengineering pays non établi dans la noticeUniversité ou école supérieure
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College Park GlycoT Therapeutics pays non établi dans la noticeUniversité ou école supérieure
Max Planck Institute for Heart and Lung Research, George Mason University et Department of Chemistry and Biochemistry — University of Maryland, avec 5 autres affiliations.
Une affiliation ne permet pas de déduire la nationalité d’un auteur.