Inhibition binding studies of glycodendrimer-lectin interactions using surface plasmon resonance.

Understanding protein-carbohydrate interactions is essential for elucidating biological pathways and cellular mechanisms but is often difficult due to the prevalence of multivalent interactions. Here, we evaluate the multivalent glycodendrimer framework as a means to describe the inhibition potency of multivalent mannose-functionalized dendrimers using surface plasmon resonance (SPR). Using highly robust, mannose-functionalized dithiol self-assembled monolayers on gold surfaces, we found that glycodendrimers were efficient inhibitors of protein-carbohydrate interactions. IC(50) values ranging from 260 nM to 13 nM were obtained for mannose-functionalized dendrimers with Concanavalin A.