Breaking the Limits in Analyzing Carbohydrate Recognition by NMR Spectroscopy: Resolving Branch‐Selective Interaction of a Tetra‐Antennary N‐Glycan with Lectins. Issue 47 (24th October 2017)

• Record Type: Journal Article
• Authors: Canales, Angeles; Boos, Irene; Perkams, Lukas; Karst, Lukas; Luber, Thomas; Karagiannis, Theodoros; Domínguez, Gemma; Cañada, F. Javier; Pérez‐Castells, Javier; Häussinger, Daniel; Unverzagt, Carlo; Jiménez‐Barbero, Jesus
• Is Part Of: Angewandte Chemie international edition. Volume 56:Issue 47(2017)
• Page Start: 14987
• Page End: 14991
• Publication Date: 2017-10-24
• Subjects: glycans -- lectins -- molecular recognition -- NMR spectroscopy -- paramagnetism; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201709130
• Languages: English
• ISSNs: 1433-7851

Abstract

Abstract: 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). Abstract : Finally resolved : For the first time, the direct identification of all four branches of a complex tetra‐antennary N ‐glycan by paramagnetic NMR spectroscopy is possible. The unprecedented resolution allowed an in‐depth characterization of the conformations and molecular recognition patterns of this complex oligosaccharide.