Recognition between a divalent sialyl molecule and wheat germ agglutinin

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Title:	Recognition between a divalent sialyl molecule and wheat germ agglutinin
Authors:	Yu, YP (Yu, Yi-Ping) Wu, AT (Wu, An-Tai) Zou, W (Zou, Wei) Chen, CS (Chen, Chien-Sheng) Wu, SH (Wu, Shih-Hsiung)
Contributors:	食營系
Keywords:	Sialic acid Wheat germ agglutinin Surface plasmon resonance Isothermal titration calorimetry Molecular modeling
Date:	2009
Issue Date:	2011-11-28 15:31:28 (UTC+8)
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 10(7) by surface plasmon resonance. (C) 2009 Elsevier Ltd. All rights reserved.
Appears in Collections:	[Department of Food and Nutrition ] journal articles

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