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 107 by surface plasmon resonance.
All Science Journal Classification (ASJC) codes
- Drug Discovery
- Organic Chemistry