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

Authors


  • 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).

Abstract

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.

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