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Mimics of Ganglioside GM1 as Cholera Toxin Ligands: Replacement of the GalNAc Residue.

✍ Scribed by Anna Bernardi; Daniela Arosio; Leonardo Manzoni; Diego Monti; Helena Posteri; Donatella Potenza; Silvia Mari; Jesus Jimenez-Barbero

Publisher: John Wiley and Sons
Year: 2003
Weight: 56 KB
Volume: 34
Category: Article
ISSN: 0931-7597
DOI: 10.1002/chin.200326213

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Ganglioside G M1 is the receptor for cholera toxin on cell surfaces, and the binding of cholera toxin to G M1 immobilized on microtitre plates has been reported previously by several authors as an assay for the toxin (G M1 -ELISA). This assay has been examined in detail. Results were independent of

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## Abstract The solution dynamics of the oligosaccharide moiety of ganglioside G~M1~ have been determined by use of a combination of ^1^H rotating frame Overhauser effect measurements and restrained molecular dynamics simulations, It is found that the Galβ1‐3 and NeuNAc moieties which are primarily