What does this research mean for the field?

O-glycosylation induces pronounced compaction of mucin-derived glycopeptides in the gas phase after desolvation, contrasting with their stiffening in solution and highlighting the critical role of hydration in stabilizing glycopeptide conformations. Novelty: ClaimNovelty.NOVEL_FINDING. Consensus alignment: ConsensusAlignment.NEUTRAL.

What question did this study set out to answer?

To investigate how O-glycosylation alters the gas-phase conformations of MUC5AC mucin-derived model peptides following desolvation.

August 25, 2026Analytical ChemistryOpen Access

Studying Mucin-Derived O -Glycopeptides with Gas-Phase FRET

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Authors

KGKim Greis AGArseniy Galashov LBLyna Bourehil

Discussion

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Overview

Spectroscopic analysis reveals that O-glycosylation induces structural compaction in desolvated MUC5AC peptides, indicating that hydration is essential for stabilizing glycopeptide conformation.

Key Points

To investigate how O-glycosylation alters the gas-phase conformations of MUC5AC mucin-derived model peptides following desolvation.
Synthesized 26-residue MUC5AC-derived model peptides containing either zero or six GalNAc residues.
Evaluated gas-phase structural dimensions and charge states using gas-phase Förster resonance energy transfer (FRET) combined with ion mobility-mass spectrometry.
O-glycosylation induced pronounced, charge-state-dependent structural compaction in desolvated gas-phase peptides, in contrast to the backbone stiffening observed in solution.
Glycopeptides with Thr-glycosylation adopted conformations that were less compact or of similar size compared to those with Ser-glycosylation.

Cite This Study

Greis et al. (2026) studied this question.

synapsesocial.com/papers/6a8d4a15e8bd2413309bbe91 https://doi.org/10.1021/acs.analchem.6c01957

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August 25, 2026Analytical ChemistryOpen Access

Studying Mucin-Derived O -Glycopeptides with Gas-Phase FRET

View Full Paper

Ask AI

Bookmark

Authors

KGKim Greis AGArseniy Galashov LBLyna Bourehil

Discussion

Member takes

Overview

Spectroscopic analysis reveals that O-glycosylation induces structural compaction in desolvated MUC5AC peptides, indicating that hydration is essential for stabilizing glycopeptide conformation.

Key Points

To investigate how O-glycosylation alters the gas-phase conformations of MUC5AC mucin-derived model peptides following desolvation.
Synthesized 26-residue MUC5AC-derived model peptides containing either zero or six GalNAc residues.
Evaluated gas-phase structural dimensions and charge states using gas-phase Förster resonance energy transfer (FRET) combined with ion mobility-mass spectrometry.
O-glycosylation induced pronounced, charge-state-dependent structural compaction in desolvated gas-phase peptides, in contrast to the backbone stiffening observed in solution.
Glycopeptides with Thr-glycosylation adopted conformations that were less compact or of similar size compared to those with Ser-glycosylation.

Cite This Study

Greis et al. (2026) studied this question.

synapsesocial.com/papers/6a8d4a15e8bd2413309bbe91 https://doi.org/10.1021/acs.analchem.6c01957

View Full Paper

Ask AI

Bookmark