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 journalArticle

3 Citations (Scopus)

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 107 by surface plasmon resonance.

Original languageEnglish
Pages (from-to)6130-6132
Number of pages3
JournalTetrahedron Letters
Volume50
Issue number45
DOIs
Publication statusPublished - 2009 Nov 11

Fingerprint

Neuraminic Acids
Wheat Germ Agglutinins
Molecules
Surface Plasmon Resonance
Surface plasmon resonance
Lectins
Scaffolds
Databases
Proteins

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Drug Discovery
  • Organic Chemistry

Cite this

Yu, Yi Ping ; Wu, An Tai ; Zou, Wei ; Chen, Chien Sheng ; Wu, Shih Hsiung. / Recognition between a divalent sialyl molecule and wheat germ agglutinin. In: Tetrahedron Letters. 2009 ; Vol. 50, No. 45. pp. 6130-6132.
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Recognition between a divalent sialyl molecule and wheat germ agglutinin. / Yu, Yi Ping; Wu, An Tai; Zou, Wei; Chen, Chien Sheng; Wu, Shih Hsiung.

In: Tetrahedron Letters, Vol. 50, No. 45, 11.11.2009, p. 6130-6132.

Research output: Contribution to journalArticle

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