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Chemoenzymatic synthesis of biotin-appended analogues of gangliosidesGM2, GM1, GD1a and GalNAc-GD1a for solid-phase applications and improved ELISA tests
Aliaksei V. Pukin,Dion E. A. Florack,Denis Brochu,Barend van Lagen,Gerben M. Visser,Tom Wennekes,Michel Gilbert,Han Zuilhof
Organic & Biomolecular Chemistry Pub Date : 05/18/2011 00:00:00 , DOI:10.1039/C1OB00009H
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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