Abstract
Fucose migration reactions represent a substantial challenge in the analysis of fucosylated glycan structures by mass spectrometry. In addition to the well-established observation of transposed fucose residues in glycan-dissociation product ions, recent experiments show that the rearrangement can also occur in intact glycan ions. These results suggest a low-energy barrier for migration of the fucose residue and broaden the relevance of fucose migration to include other types of mass spectrometry experiments, including ion mobility-mass spectrometry and ion spectroscopy. In this work, we utilize cold-ion infrared spectroscopy to provide further insight into glycan scrambling in intact glycan ions. Our results show that the mobility of the proton is a prerequisite for the migration reaction. For the prototypical fucosylated glycans Lewis x and blood group antigen H-2, the formation of adduct ions or the addition of functional groups with variable proton affinity yields significant differences in the infrared spectra. These changes correlate well with the promotion or inhibition of fucose migration through the presence or absence of a mobile proton.
Highlights
Glycans are among the most abundant biomacromolecules in living organisms and are essential in a variety of biological functions, such as cell-signaling and molecular recognition [1, 2]
Our results clearly show that a mobile proton at a specific site of the molecule is required for fucose migration
The Lewis y (Ley)-series consists of the tetrasaccharide Ley and the two trisaccharides blood group antigen H-2 (BG-H2) and Lewis x (Lex) that are substructures of Ley (Fig. 3a; Electronic Supplementary Material (ESM) Fig. S1)
Summary
Glycans are among the most abundant biomacromolecules in living organisms and are essential in a variety of biological functions, such as cell-signaling and molecular recognition [1, 2].
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
