Abstract
Unnatural, NMR- and MRI-active fluorinated sugar probes, designed and synthesised to bind to the pathogenic protein TgMIC1 from Toxoplasma gondii, were found to display binding potency equal to and above that of the natural ligand. Dissection of the binding mechanism and modes, including the first X-ray crystal structures of a fluoro-oligosaccharide bound to a lectin, demonstrate that it is possible to create effective fluorinated probe ligands for the study of, and perhaps intervention in, sugar-protein binding events.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Carbohydrate Metabolism
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Cell Adhesion
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Cell Adhesion Molecules / chemistry
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Cell Adhesion Molecules / metabolism
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Crystallography, X-Ray
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Disaccharides / chemical synthesis
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Disaccharides / chemistry
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Halogenation*
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Molecular Probes / chemical synthesis
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Molecular Probes / chemistry*
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Molecular Probes / metabolism*
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Oligosaccharides / chemical synthesis
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Oligosaccharides / chemistry*
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Oligosaccharides / metabolism*
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Protozoan Proteins / chemistry
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Protozoan Proteins / metabolism
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Receptors, Cell Surface / metabolism
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Toxoplasma / cytology*
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Toxoplasma / metabolism
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Toxoplasmosis / parasitology*
Substances
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Cell Adhesion Molecules
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Disaccharides
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MIC1 protein, Toxoplasma gondii
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Molecular Probes
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Oligosaccharides
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Protozoan Proteins
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Receptors, Cell Surface
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saccharide-binding proteins