Abstract
Structural divalency between a designed N-acetyl-neuraminic acid (NeuAc)-containing molecule and lectin wheat germ agglutinin (WGA) is investigated. The sialyl molecule was designed based on the NeuAc–WGA complex in the Protein Data Bank and featured polyethylene glycol linkers connecting to an aromatic scaffold. Our results elucidate the divalent recognition association constant between WGA and the multivalent-NeuAc molecules to be 10 7 by surface plasmon resonance.
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