Recognition between a divalent sialyl molecule and wheat germ agglutinin

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DOIResolve DOI: http://doi.org/10.1016/j.tetlet.2009.08.073
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TypeArticle
Journal titleTetrahedron Letters
Volume50
Issue45
Pages61306132; # of pages: 3
SubjectSialic acid; Wheat germ agglutinin; Surface plasmon resonance; Isothermal titration calorimetry; Molecular modeling
AbstractStructural 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.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada (NRC-CNRC); NRC Institute for Biological Sciences
Peer reviewedYes
NPARC number15329250
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Record identifier1b358419-a306-4fd4-a66b-13ad312daafd
Record created2010-05-21
Record modified2016-05-09
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