HOT: glycosyldisulfide lectin ligands

S-glycosides are resistant to hydrolytic cleavage, which gives them a distinct pharmacological advantage over O-glycosides as ligands for lectins, but inherently present different biological activity.  This HOT article evaluates the ability of dithiodigalactoside (DTDG) – which was identified through a dynamic combinatorial library approach in a previous study – to protect human cells from toxin binding.

Jésus Jiménez-Barbero, CSIC, and an international team of researchers show that DTDG is capable of selecting between the mistletoe toxin and human lectins and conclude that glycosyldisulfides have potential as chemical platform for inhibitor design.

Interested? The article is free to download for the next 4 weeks:

Symmetric dithiodigalactoside: strategic combination of binding studies and detection of selectivity between a plant toxin and human lectins
Sonsoles Martín-Santamaría, Sabine André, Eliza Buzamet, Rémi Caraballo, Gloria Fernández-Cureses, Maria Morando, João P. Ribeiro, Karla Ramírez-Gualito, Beatriz de Pascual-Teresa, F. Javier Cañada, Margarita Menéndez, Olof Ramström, Jesús Jiménez-Barbero, Dolores Solís and Hans-Joachim Gabius
Org. Biomol. Chem., 2011, Advance Article
DOI: 10.1039/C0OB01235A

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