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Issue 23, 2014
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19F NMR spectroscopy monitors ligand binding to recombinantly fluorine-labelled bx from human protein disulphide isomerase (hPDI)

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Abstract

We report a protein-observe 19F NMR-based ligand titration binding study of human PDI b′x with Δ-somatostatin that also emphasises the need to optimise recombinant protein fluorination when using 5- or 6-fluoroindole. This study highlights a recombinant preference for 5-fluoroindole over 6-fluoroindole; most likely due to the influence of fluorine atomic packing within the folded protein structure. Fluorination affords a single 19F resonance probe to follow displacement of the protein x-linker as ligand is titrated and provides a dissociation constant of 23 ± 4 μM.

Graphical abstract: 19F NMR spectroscopy monitors ligand binding to recombinantly fluorine-labelled b′x from human protein disulphide isomerase (hPDI)

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Publication details

The article was received on 02 Apr 2014, accepted on 29 Apr 2014 and first published on 29 Apr 2014


Article type: Communication
DOI: 10.1039/C4OB00699B
Citation: Org. Biomol. Chem., 2014,12, 3808-3812
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    19F NMR spectroscopy monitors ligand binding to recombinantly fluorine-labelled bx from human protein disulphide isomerase (hPDI)

    R. Curtis-Marof, D. Doko, M. L. Rowe, K. L. Richards, R. A. Williamson and M. J. Howard, Org. Biomol. Chem., 2014, 12, 3808
    DOI: 10.1039/C4OB00699B

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