Recognition between a divalent sialyl molecule and wheat germ agglutinin

Yi Ping Yu, An Tai Wu, Wei Zou, Chien Sheng Chen, Shih Hsiung Wu

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)6130-6132
Number of pages3
JournalTetrahedron Letters
Issue number45
Publication statusPublished - 2009 Nov 11

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Drug Discovery
  • Organic Chemistry

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