Communication

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

  1. Yann Ferrand Dr.1,
  2. Emmanuel Klein Dr.1,
  3. Nicholas P. Barwell1,
  4. Matthew P. Crump Dr.1,
  5. Jesus Jiménez-Barbero Prof.2,
  6. Cristina Vicent Dr.3,
  7. Geert-Jan Boons Prof.4,
  8. Sampat Ingale4,
  9. Anthony P. Davis Prof.1

Article first published online: 15 DEC 2008

DOI: 10.1002/anie.200804905

Issue

Angewandte Chemie International Edition

Angewandte Chemie International Edition

Volume 48, Issue 10, pages 1775–1779, February 23, 2009

Additional Information

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

Author Information

  1. 1

    School of Chemistry, University of Bristol, Cantock's Close, Bristol, BS8 1TS (UK), Fax: (+44) 117-929-8611

  2. 2

    Centro de Investigaciones Biológicas, CSIC, Madrid (Spain)

  3. 3

    Instituto de Química Organica, CSIC, Madrid (Spain)

  4. 4

    Complex Carbohydrate Research Center, University of Georgia (USA)

  1. †

    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).

Publication History

  1. Issue published online: 17 FEB 2009
  2. Article first published online: 15 DEC 2008
  3. Manuscript Received: 7 OCT 2008

Funded by

  • EPSRC
  • National Cancer Institute
  • NIH

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Keywords:

  • biomimetic hosts;
  • carbohydrates;
  • molecular recognition;
  • receptors;
  • supramolecular chemistry

Abstract

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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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