Title of article
Recognition between a divalent sialyl molecule and wheat germ agglutinin
Author/Authors
Yu، نويسنده , , Yiping and Wu، نويسنده , , An-Tai and Zou، نويسنده , , Wei and Chen، نويسنده , , Chien-Sheng and Wu، نويسنده , , Shih-Hsiung، نويسنده ,
Issue Information
هفته نامه با شماره پیاپی سال 2009
Pages
3
From page
6130
To page
6132
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.
Keywords
Isothermal titration calorimetry , molecular modeling , Sialic acid , wheat germ agglutinin , surface plasmon resonance
Journal title
Tetrahedron Letters
Serial Year
2009
Journal title
Tetrahedron Letters
Record number
1866380
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