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

Curtis-Marof, Rose, Doko, Denisa, Rowe, Michelle L., Richards, Kirsty, Williamson, Richard A., Howard, Mark J. (2014) 19F NMR spectroscopy monitors ligand binding to recombinantly fluorine-labelled b'x from human protein disulphide isomerase (hPDI). Organic & Biomolecular Chemistry, 12 (23). pp. 3808-3812. ISSN 1477-0520. E-ISSN 1477-0539. (doi:10.1039/C4OB00699B)

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http://dx.doi.org/10.1039/C4OB00699B

Abstract

We report a protein-observe (19)F NMR-based ligand titration binding study of human PDI b'x with ?-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 ?M.

Item Type: Article
DOI/Identification number: 10.1039/C4OB00699B
Subjects: Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
Divisions: Faculties > Sciences > School of Biosciences
Faculties > Sciences > School of Biosciences > Protein Science Group
Depositing User: M.J. Howard
Date Deposited: 06 Nov 2014 17:15 UTC
Last Modified: 29 May 2019 13:23 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/44132 (The current URI for this page, for reference purposes)
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