Using dendrimers functionalized with mannose, glucose, and galactose to study multivalent protein-carbohydrate interactions

CARB 24

Mark L. Wolfenden, mwolfenden2000@yahoo.com, Shane L. Mangold, m0078477@hotmail.com, and Mary J. Cloninger, mcloninger@chemistry.montana.edu. Department of Chemistry and Biochemistry and Center for Bioinspired Nanomaterials, Montana State University, Bozeman, MT 59717
Multivalent protein-carbohydrate interactions on the cell surface play key roles in many cellular processes including the adhesion and metastasis of cancer cells. Here, the heterogeneous functionalization of PAMAM dendrimers with combinations of mannose, glucose, and galactose is described. Binding assays with Concanavalin A, a mannose-binding model protein, are described. Binding studies with a monomeric Concanavalin A derivative are also reported. Our results with dendrimers that have a combination of monosaccharide endgroups suggest that the degree of lectin clustering and the affinity of the dendrimers for the lectins can be predictably attenuated. Our results with monomeric Concanavalin A help to define the limits within which we can apply these predictions to dendrimer design.