Abstract
We report a protein-observe (19)F 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 (19)F resonance probe to follow displacement of the protein x-linker as ligand is titrated and provides a dissociation constant of 23 ± 4 μM.
Highlights
19F NMR spectroscopy monitors ligand binding to recombinantly fluorine-labelled b’x from human protein disulphide isomerase†
Protein disulphide isomerase (PDI) is a key enzyme responsible for the formation of native disulphide bonds in proteins that enter the secretory pathway of eukaryotic cells
The ability of PDI to combine redox and molecular chaperone-like activities allows it to bind to partly structured folding intermediates and to catalyse simultaneously protein folding and associated native disulphide bond formation.[3]
Summary
19F NMR spectroscopy monitors ligand binding to recombinantly fluorine-labelled b’x from human protein disulphide isomerase (hPDI)†. We report a protein-observe 19F NMR-based ligand titration binding study of human PDI b’x with Δ-somatostatin that emphasises the need to optimise recombinant protein fluorination when using 5- or 6-fluoroindole.
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