Glycodendrimers and Modified ELISAs: Tools to Elucidate Multivalent Interactions of Galectins 1 and 3

Molecules

Mark Wolfenden²  Jonathan Cousin²  Pratima Nangia-Makker¹  Avraham Raz¹  Mary Cloninger² 

[1] The Departments of Oncology and Pathology, School of Medicine, Wayne State University, Detroit, MI 48201, USA; E-Mails:;Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT 59717, USA; E-Mails:

关键词: ELISA;    galectin-1;    galectin-3;    glycodendrimer;    dendrimer;    multivalent;   

DOI  :  10.3390/molecules20047059

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2015 by the authors; licensee MDPI, Basel, Switzerland.