Binding of monomeric and dimeric Concanavalin A to mannose-functionalized dendrimers.
Because of the central role of Concanavalin A (Con A) in the study of protein-carbohydrate interactions, a thorough understanding of the multivalent functions of Con A is imperative. Here, the association of monomeric and dimeric derivatives of Con A with mannose-functionalized generation two through six PAMAM dendrimers is reported. Hemagglutination assay results indicate relatively low activity of the dendrimers for monomeric Con A, with small increases as the dendrimer generation increases. Isothermal titration microcalorimetry experiments indicate monovalent binding by the dendrimers with monomeric Con A and divalent binding by the dendrimers with dimeric Con A. Continuous (and comparable) but narrowing increases in enthalpy and entropy and the slight increase in association constants with monomeric Con A as the dendrimer generation increases suggest favorable proximity effects on binding. Both the hemagglutination assay and the calorimetry experiments suggest that statistical binding enhancements can be observed with monomeric Con A. The results described here should allow for a more quantitative evaluation of the enhancements that are often observed in protein-carbohydrate interactions for glycosylated frameworks binding to Con A.