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A Triazatruxene-Based Glycocluster as a Fluorescent Sensor for Concanavalin A

Authors

  • Dr. Ke-Rang Wang,

    1. Key Laboratory of Chemical Biology of Hebei Province, College of Chemistry and Environmental Science, Hebei University, Baoding 071002 (P.R. China), Fax: (+86) 312-5079-1116
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  • Yue-Qing Wang,

    1. Key Laboratory of Chemical Biology of Hebei Province, College of Chemistry and Environmental Science, Hebei University, Baoding 071002 (P.R. China), Fax: (+86) 312-5079-1116
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  • Hong-Wei An,

    1. Key Laboratory of Chemical Biology of Hebei Province, College of Chemistry and Environmental Science, Hebei University, Baoding 071002 (P.R. China), Fax: (+86) 312-5079-1116
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  • Jin-Chao Zhang,

    1. Key Laboratory of Chemical Biology of Hebei Province, College of Chemistry and Environmental Science, Hebei University, Baoding 071002 (P.R. China), Fax: (+86) 312-5079-1116
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  • Prof. Dr. Xiao-Liu Li

    Corresponding author
    1. Key Laboratory of Chemical Biology of Hebei Province, College of Chemistry and Environmental Science, Hebei University, Baoding 071002 (P.R. China), Fax: (+86) 312-5079-1116
    • Key Laboratory of Chemical Biology of Hebei Province, College of Chemistry and Environmental Science, Hebei University, Baoding 071002 (P.R. China), Fax: (+86) 312-5079-1116
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Abstract

A new triazatruxene-based fluorescent glycocluster has been designed, synthesized, and fully characterized by NMR spectroscopy and mass spectrometry. Furthermore, its specific and selective binding properties with concanavalin A (Con A) have been investigated by fluorescence spectroscopy, circular dichroism (CD) spectroscopy, and turbidity assay. The obtained results showed that the multivalent mannose-modified triazatruxene exhibited specific binding with Con A, but no binding to peanut agglutinin (PNA) lectin or bovine serum albumin (BSA), corresponding to a two-orders-of-magnitude higher affinity than that of monovalent mannose ligands. Most interestingly, a fluorescence enhancement of the triazatruxene-based glycocluster was observed upon binding with Con A because of hydrophobic interactions involving sites close to the triazatruxene moiety. Furthermore, the inhibitory ability of the triazatruxene-based glycocluster against ORN178- induced haemagglutination has been investigated by haemagglutination inhibition assay. The results indicated selective binding with ORN178.

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