Glycodendrimers and modified ELISAs: Tools to elucidate multivalent interactions of galectins 1 and 3

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Abstract

Multivalent protein-carbohydrate interactions that are mediated by sugar-binding proteins, i.e., lectins, have been implicated in a myriad of intercellular recognition processes associated with tumor progression such as galectin-mediated cancer cellular migration/metastatic processes. Here, using a modified ELISA, we show that glycodendrimers bearing mixtures of galactosides, lactosides, and N-acetylgalactosaminosides, galectin-3 ligands, multivalently affect galectin-3 functions. We further demonstrate that lactose functionalized glycodendrimers multivalently bind a different member of the galectin family, i.e., galectin-1. In a modified ELISA, galectin-3 recruitment by glycodendrimers was shown to directly depend on the ratio of low to high affinity ligands on the dendrimers, with lactose-functionalized dendrimers having the highest activity and also binding well to galectin-1. The results depicted here indicate that synthetic multivalent systems and upfront assay formats will improve the understanding of the multivalent function of galectins during multivalent protein carbohydrate recognition/interaction.

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Wolfenden, M., Cousin, J., Nangia-Makker, P., Raz, A., & Cloninger, M. (2015). Glycodendrimers and modified ELISAs: Tools to elucidate multivalent interactions of galectins 1 and 3. Molecules, 20(4), 7059–7096. https://doi.org/10.3390/molecules20047059

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