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.
Schlick
Kristian H
KH
Department of Chemistry and Biochemistry, 103 Chemistry and Biochemistry Building, Montana State University, Bozeman, MT 59717.
Cloninger
Mary J
MJ
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