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Issue 16, 2011
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Chemoenzymatic synthesis of biotin-appended analogues of gangliosides GM2, GM1, GD1a and GalNAc-GD1a for solid-phase applications and improved ELISA tests

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Abstract

Biotinylated analogues of gangliosides GM2, GM1, GD1a and GalNAc-GD1a were synthesized in high yields using glycosyltransferases from Campylobacter jejuni. The presence of a biotin moiety in the aglycone part of these mimics allows for attachment of these materials onto various streptavidin-coated surfaces. Analysis of the interaction of biotin-appended GM1 with the B subunit of Escherichia coli heat-labile enterotoxin performed in a modified ELISA procedure shows the potential of this compound to replace the natural GM1 in toxin detection.

Graphical abstract: Chemoenzymatic synthesis of biotin-appended analogues of gangliosides GM2, GM1, GD1a and GalNAc-GD1a for solid-phase applications and improved ELISA tests

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Publication details

The article was received on 04 Jan 2011, accepted on 18 May 2011 and first published on 18 May 2011


Article type: Paper
DOI: 10.1039/C1OB00009H
Citation: Org. Biomol. Chem., 2011,9, 5809-5815
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    Chemoenzymatic synthesis of biotin-appended analogues of gangliosides GM2, GM1, GD1a and GalNAc-GD1a for solid-phase applications and improved ELISA tests

    A. V. Pukin, D. E. A. Florack, D. Brochu, B. van Lagen, G. M. Visser, T. Wennekes, M. Gilbert and H. Zuilhof, Org. Biomol. Chem., 2011, 9, 5809
    DOI: 10.1039/C1OB00009H

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