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<p>Glycosaminoglycans use positional sulfation to encode binding specificity onto its sequence. Understanding these sulfation patterns constitute a major challenge. Previous studies hinted that sulfate groups can migrate along glycans during collision-induced dissociation in mass spectrometry (MS) experiments, forming isomeric fragments that can lead to incorrect structural assignments. We use ion-mobility – mass spectrometry to investigate the mechanism of this phenomenon in heparin sulfate disaccharides. The sulfate group migrates from the non-reducing to reducing end of the sugar, and the degree of migration does not depend on the structure of the label. The migration product has a sulfate group attached to either 6<i>O</i>- or 3<i>O</i>-position of GlcNAc, and the migration mechanism consists of multiple steps, with the sulfate group first shifting from the iduronic acid to the 6<i>O</i>-position of GlcNAc, and next to the 3<i>O</i>-position. The presented data offer insight into the complexity and unpredictability of sulfated sugar fragmentation in tandem MS and extensive investigations is required to determine whether this represents a singular case or a general phenomenon characteristic of deprotonated sulfated glycans.</p><p></p>

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Mechanistic study on the sulfate migration in glycosaminoglycans during MS fragmentation

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年2月14日

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  • Lukasz Polewski,
  • Murat Yaman,
  • Matko Tokić,
  • Mateusz Marianski,
  • Kevin Pagel

摘要

Glycosaminoglycans use positional sulfation to encode binding specificity onto its sequence. Understanding these sulfation patterns constitute a major challenge. Previous studies hinted that sulfate groups can migrate along glycans during collision-induced dissociation in mass spectrometry (MS) experiments, forming isomeric fragments that can lead to incorrect structural assignments. We use ion-mobility – mass spectrometry to investigate the mechanism of this phenomenon in heparin sulfate disaccharides. The sulfate group migrates from the non-reducing to reducing end of the sugar, and the degree of migration does not depend on the structure of the label. The migration product has a sulfate group attached to either 6O- or 3O-position of GlcNAc, and the migration mechanism consists of multiple steps, with the sulfate group first shifting from the iduronic acid to the 6O-position of GlcNAc, and next to the 3O-position. The presented data offer insight into the complexity and unpredictability of sulfated sugar fragmentation in tandem MS and extensive investigations is required to determine whether this represents a singular case or a general phenomenon characteristic of deprotonated sulfated glycans.