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) (KAR id:44132)

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Official URL: 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:	Divisions > Division of Natural Sciences > Biosciences
Depositing User:	M.J. Howard
Date Deposited:	06 Nov 2014 17:15 UTC
Last Modified:	05 Nov 2024 10:28 UTC
Resource URI:	https://kar.kent.ac.uk/id/eprint/44132 (The current URI for this page, for reference purposes)

University of Kent Author Information

Rowe, Michelle L..

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Williamson, Richard A..

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Howard, Mark J..

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