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Recognition between a divalent sialyl molecule and wheat germ agglutinin |
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| Authors: | Yi-Ping Yu Wei Zou Shih-Hsiung Wu |
| Affiliation: | a Department of Food, Health and Nutrition Science, Chinese Culture University, Taipei 11114, Taiwan b Department of Chemistry, National Changhua University of Education, Changhua 50058, Taiwan, ROC c Institute for Biological Sciences, National Research Council of Canada, 100 Sussex Drive, Ottawa, Ontario, Canada K1A 0R6 d Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan |
| 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: | Sialic acid Wheat germ agglutinin Surface plasmon resonance Isothermal titration calorimetry Molecular modeling |
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