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Fluorinated Carbohydrates as Lectin Ligands: Synthesis of OH/F‐Substituted N ‐Glycan Core Trimannoside and Epitope Mapping by 2D STD‐TOCSYreF NMR spectroscopy
Author(s) -
Diercks Tammo,
Infantino Angela Simona,
Unione Luca,
JiménezBarbero Jesús,
Oscarson Stefan,
Gabius HansJoachim
Publication year - 2018
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201803217
Subject(s) - glycan , chemistry , nuclear magnetic resonance spectroscopy , mannose , two dimensional nuclear magnetic resonance spectroscopy , stereochemistry , spectroscopy , lectin , heteronuclear single quantum coherence spectroscopy , crystallography , biochemistry , glycoprotein , physics , quantum mechanics
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.