Advanced Materials

Glyconanomaterials: Synthesis, Characterization, and Ligand Presentation

Authors

  • Xin Wang,

    1. Department of Chemistry Portland State University P.O. Box 751, Portland, Oregon, 97207-0751 (USA)
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  • Olof Ramström,

    Corresponding author
    1. Department of Chemistry Portland State University P.O. Box 751, Portland, Oregon, 97207-0751 (USA)
    2. Department of Chemistry KTH - Royal Institute of Technology Teknikringen 30, Stockholm, S-10044 (Sweden)
    • Department of Chemistry Portland State University P.O. Box 751, Portland, Oregon, 97207-0751 (USA).
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  • Mingdi Yan

    Corresponding author
    1. Department of Chemistry Portland State University P.O. Box 751, Portland, Oregon, 97207-0751 (USA)
    • Department of Chemistry Portland State University P.O. Box 751, Portland, Oregon, 97207-0751 (USA).
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Abstract

Glyconanomaterials, nanomaterials carrying surface-tethered carbohydrate ligands, have emerged and demonstrated increasing potential in biomedical imaging, therapeutics, and diagnostics. These materials combine the unique properties of nanometer-scale objects with the ability to present multiple copies of carbohydrate ligands, greatly enhancing the weak affinity of individual ligands to their binding partners. Critical to the performance of glyconanomaterials is the proper display of carbohydrate ligands, taking into consideration of the coupling chemistry, the type and length of the spacer linkage, and the ligand density. This article provides an overview of the coupling chemistry for attaching carbohydrate ligands to nanomaterials, and discusses the need for thorough characterization of glyconanomaterials, especially quantitative analyses of the ligand density and binding affinities. Using glyconanoparticles synthesized by a versatile photocoupling chemistry, methods for determining the ligand density by colorimetry and the binding affinity with lectins by a fluorescence competition assay are determined. The results show that the multivalent presentation of carbohydrate ligands significantly enhances the binding affinity by several orders of magnitude in comparison to the free ligands in solution. The effect is sizeable even at low surface ligand density. The type and length of the spacer linkage also affect the binding affinity, with the longer linkage promoting the association of bound ligands with the corresponding lectins.

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