Synthetic glycoprotein conjugates were synthesized through the polymerization of glycomonomers (mannose and/or galactose acrylate) directly from a protein macroinitiator. This design combines the multivalency of polymer structures with 3D display of saccharides randomly arranged around a central protein structure. The conjugates were tested for their interaction with mannose binding lectin (MBL), a key protein of immune complement. Increasing mannose number (controlled through polymer chain length) and density (controlled through comonomer feed ratio of mannose versus galactose) result in greater interaction with MBL. Most significantly, mannose glycopolymers displayed in a multivalent and 3D configuration from the protein exhibit dramatically enhanced interaction with MBL compared to linear glycopolymer chains with similar total valency but lacking 3D display. These findings demonstrate the importance of the 3D presentation of ligand structures for designing biomimetic materials.
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