Send to

Choose Destination
Chemistry. 2018 Oct 22;24(59):15761-15765. doi: 10.1002/chem.201803217. Epub 2018 Oct 1.

Fluorinated Carbohydrates as Lectin Ligands: Synthesis of OH/F-Substituted N-Glycan Core Trimannoside and Epitope Mapping by 2D STD-TOCSYreF NMR spectroscopy.

Author information

NMR Facility, CIC bioGUNE, Bizkaia Technology Park, Bld 800, 48170, Derio, Spain.
Centre for Synthesis and Chemical Biology, University College Dublin, Belfield, Dublin 4, Ireland.
Molecular Recognition and Host-Pathogen Interactions, CIC bioGUNE, Bizkaia Technology Park, Bld 800, 48170, Derio, Spain.
Tierärztliche Fakultät, Institut für Physiologische Chemie, Ludwig-Maximilians-Universität München, Veterinärstr. 13, 80539, München, Germany.


Glycan-protein interactions play an important role in a broad range of physiological processes, raising interest to elucidate the structural interplay. Yet, their dynamic nature limits the analysis by crystallography, whereas NMR spectroscopy suffers from the low 1 H dispersion of glycans. Therefore, their sparse fluorination and NMR screening by 1D Saturation Transfer Difference with relay to 19 F (STDreF) was previously proposed to exploit the superior dispersion in 19 F NMR spectroscopy. A new 2D STD-TOCSYreF experiment is presented here that enables comprehensive epitope mapping of fluorinated glycans by combining the spectral resolution of 19 F with the spatial resolution and coverage of 1 H. For an illustration, the 2-deoxy-2-fluoro derivative of the N-glycan core trimannoside was synthesised and its recognition of Pisum sativum agglutinin by either of the two terminal mannose residues was confirmed. Going beyond the crystallographic information, the 2D STD-TOCSYreF spectrum moreover visualised collateral contacts from the branching mannose and allowed to assess the ratio of both co-existing binding modes through the α1,3- (67 %) and α1,6-linked (33 %) terminal mannose moieties.


19F NMR spectroscopy; epitope mapping; fluorine; glycan; sugar code


Supplemental Content

Loading ...
Support Center