This work was supported by the EU (HPRN-CT-2002-00190), the EPSRC (EP/D060192/1), the National Cancer Institute of the NIH (RO1 CA88986), and the Ministry of Science and Innovation of Spain (CTQ2006-10874-C02).
A Synthetic Lectin for O-Linked β-N-Acetylglucosamine†
Article first published online: 15 DEC 2008
Copyright © 2009 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 48, Issue 10, pages 1775–1779, February 23, 2009
How to Cite
Ferrand, Y., Klein, E., Barwell, Nicholas P., Crump, Matthew P., Jiménez-Barbero, J., Vicent, C., Boons, G.-J., Ingale, S. and Davis, Anthony P. (2009), A Synthetic Lectin for O-Linked β-N-Acetylglucosamine. Angew. Chem. Int. Ed., 48: 1775–1779. doi: 10.1002/anie.200804905
- Issue published online: 17 FEB 2009
- Article first published online: 15 DEC 2008
- Manuscript Received: 7 OCT 2008
- National Cancer Institute
- biomimetic hosts;
- molecular recognition;
- supramolecular chemistry
Changing employment: Receptor 1 binds β-N-acetylglucosaminyl (β-GlcNAc) up to 100 times more strongly than it does glucose. This synthetic lectin shows affinities similar to wheat germ agglutinin (WGA), a natural lectin used to bind GlcNAc. Remarkably, 1 is more selective than WGA. It favors especially the glycoside unit in glycopeptide 2, a model of the serine-O-GlcNAc posttranslational protein modification.