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Thermodynamic parameters of the interaction of Urtica dioica agglutinin with N-acetylglucosamine and its oligomers

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Abstract

The interaction between Urtica dioica agglutinin (UDA) and N-acetylglucosamine (GlcNAc) and its β(1-4)-linked oligomers was studied by fluorescence titration and isothermal titration microcalorimetry. UDA possesses one significant binding site that can be measured calorimetrically. This site is composed of three subsites, each subsite accommodating one GlcNAc residue. The interaction is enthalpically driven, and the binding area of UDA is characterized by a ΔH of interaction for a given oligosaccharide considerably smaller than that of wheat germ agglutinin (WGA), despite the fact that they both belong to a family of proteins composed entirely of hevein domains. Relatively high ΔCp values of the UDA-carbohydrate interactions and more favorable entropy term compared to WGA suggest that binding of the carbohydrate ligands by UDA has a higher hydrophobic component than that of WGA.

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Authors and Affiliations

  1. Department of Biology, Johns Hopkins University, 3400 N. Charles Street, Baltimore, MD, 21218, USA

    Reiko T Lee & Yuan C Lee

  2. Institut fur Physiologische Chemie, Ludwig-Maximilians-Universitat, Veterinarstr. 13, D-80539, Munchen, Germany

    Hans-Joachim Gabius

Authors
  1. Reiko T Lee
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  2. Hans-Joachim Gabius
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  3. Yuan C Lee
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Lee, R.T., Gabius, HJ. & Lee, Y.C. Thermodynamic parameters of the interaction of Urtica dioica agglutinin with N-acetylglucosamine and its oligomers. Glycoconj J 15, 649–655 (1998). https://doi.org/10.1023/A:1006976129458

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  • DOI: https://doi.org/10.1023/A:1006976129458

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