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Wiley, Angewandte Chemie International Edition, 10(48), p. 1775-1779, 2009

DOI: 10.1002/anie.200804905

Wiley, Angewandte Chemie, 10(121), p. 1807-1811, 2009

DOI: 10.1002/ange.200804905

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A Synthetic Lectin for O-Linked β-N-Acetylglucosamine

Journal article published in 2009 by Yann Ferrand, Emmanuel Klein, Nicholas P. Barwell, Matthew P. Crump, Jesus Jiménez-Barbero ORCID, Cristina Vicent, Geert-Jan Boons ORCID, Sampat Ingale, Anthony P. Davis
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Abstract

Changing employment: Receptor 1 binds beta-N-acetylglucosaminyl (beta-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.