| Institution: | 1. Fritz-Haber-Intitut der Max-Planck-Gesellschaft, Germany;2. Department of Chemistry, University of California, Riverside, USA;3. Department of Chemistry and Biochemistry, Hunter College, The City University of New York, USA
The PhD Program in Chemistry and Biochemistry, The Graduate Center, The City University of New York, USA;4. Department of Chemistry and Biochemistry, Hunter College, The City University of New York, USA |
| Abstract: | Fucose is a signaling carbohydrate that is attached at the end of glycan processing. It is involved in a range of processes, such as the selectin-dependent leukocyte adhesion or pathogen-receptor interactions. Mass-spectrometric techniques, which are commonly used to determine the structure of glycans, frequently show fucose-containing chimeric fragments that obfuscate the analysis. The rearrangement leading to these fragments—often referred to as fucose migration—has been known for more than 25 years, but the chemical identity of the rearrangement product remains unclear. In this work, we combine ion-mobility spectrometry, radical-directed dissociation mass spectrometry, cryogenic IR spectroscopy of ions, and density-functional theory calculations to deduce the product of the rearrangement in the model trisaccharides Lewis x and blood group H2. The structural search yields the fucose moiety attached to the galactose with an α(1→6) glycosidic bond as the most likely product. |
