Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 56, Issue 47, Pages 14987-14991Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201709130
Keywords
glycans; lectins; molecular recognition; NMR spectroscopy; paramagnetism
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Funding
- Agencia Estatal de Investigacion of Spain [CTQ2016-76263-P, CTQ2015-64597-C2-1P, CTQ2015-64597-C2-2P, CTQ2015-64624-R, SEV-2016-0644]
- MINECO of Spain [CTQ2016-76263-P, CTQ2015-64597-C2-1P, CTQ2015-64597-C2-2P, CTQ2015-64624-R, SEV-2016-0644]
- Santander-Complutense University project [PR26/16-10B-3]
- Deutsche Forschungsgemeinschaft
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The biological recognition of complex-type N-glycans is part of many key physiological and pathological events. Despite their importance, the structural characterization of these events remains unsolved. The inherent flexibility of N-glycans hampers crystallization and the chemical equivalence of individual branches precludes their NMR characterization. By using a chemoenzymatically synthesized tetra-antennary N-glycan conjugated to a lanthanide binding tag, the NMR signals under paramagnetic conditions discriminated all four N-acetyl lactosamine antennae with unprecedented resolution. The NMR data revealed the conformation of the N-glycan and permitted for the first time the direct identification of individual branches involved in the recognition by two N-acetyllactosamine-binding lectins, Datura stramonium seed lectin (DSL) and Ricinus Communis agglutinin (RCA120).
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