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Issue 12, 2009
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Multivalent ligand presentation as a central concept to study intricate carbohydrate–protein interactions

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Abstract

Studying the weak binding affinities between carbohydrates and proteins has been a central theme in sustained efforts to uncover intricate details of this class of biomolecular interaction. The amphiphilic nature of most carbohydrates, the competing nature of the surrounding water molecules to a given protein receptor site and the receptor binding site characteristics led to the realization that carbohydrates are required to exert favorable interactions, primarily through clustering of the ligands. The clustering of sugar ligands has been augmented using many different innovative molecular scaffolds. The synthesis of clustered ligands also facilitates fine-tuning of the spatial and topological proximities between the ligands, so as to allow the identification of optimal molecular features for significant binding affinity enhancements. The kinetic and thermodynamic parameters have been delineated in many instances, thereby allowing an ability to correlate the multivalent presentation and the observed ligand–receptor interaction profiles. This critical review presents various multivalent ligands, synthetic and semisynthetic, and mechanisms by which the weak binding affinities are overcome, and the ligand–receptor complexation leads to significantly enhanced binding affinities (157 references).

Graphical abstract: Multivalent ligand presentation as a central concept to study intricate carbohydrate–protein interactions

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Publication details

The article was received on 23 Feb 2009 and first published on 17 Aug 2009


Article type: Critical Review
DOI: 10.1039/B815961K
Citation: Chem. Soc. Rev., 2009,38, 3463-3483

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    Multivalent ligand presentation as a central concept to study intricate carbohydrate–protein interactions

    N. Jayaraman, Chem. Soc. Rev., 2009, 38, 3463
    DOI: 10.1039/B815961K

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