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
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
Journal title :
Tetrahedron Letters
