Protein-ligand binding affinity determination by the waterLOGSY method: An optimised approach considering ligand rebinding

WaterLOGSY is a popular ligand-observed NMR technique to screen for protein-ligand interactions, yet when applied to measure dissociation constants (K(D)) through ligand titration, the results were found to be strongly dependent on sample conditions. Herein, we show that accurate K(D)s can be obtain...

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Autores principales: Huang, Renjie, Bonnichon, Arnaud, Claridge, Timothy D. W., Leung, Ivanhoe K. H.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2017
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5335602/
https://www.ncbi.nlm.nih.gov/pubmed/28256624
http://dx.doi.org/10.1038/srep43727
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author Huang, Renjie
Bonnichon, Arnaud
Claridge, Timothy D. W.
Leung, Ivanhoe K. H.
author_facet Huang, Renjie
Bonnichon, Arnaud
Claridge, Timothy D. W.
Leung, Ivanhoe K. H.
author_sort Huang, Renjie
collection PubMed
description WaterLOGSY is a popular ligand-observed NMR technique to screen for protein-ligand interactions, yet when applied to measure dissociation constants (K(D)) through ligand titration, the results were found to be strongly dependent on sample conditions. Herein, we show that accurate K(D)s can be obtained by waterLOGSY with optimised experimental setup.
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spelling pubmed-53356022017-03-07 Protein-ligand binding affinity determination by the waterLOGSY method: An optimised approach considering ligand rebinding Huang, Renjie Bonnichon, Arnaud Claridge, Timothy D. W. Leung, Ivanhoe K. H. Sci Rep Article WaterLOGSY is a popular ligand-observed NMR technique to screen for protein-ligand interactions, yet when applied to measure dissociation constants (K(D)) through ligand titration, the results were found to be strongly dependent on sample conditions. Herein, we show that accurate K(D)s can be obtained by waterLOGSY with optimised experimental setup. Nature Publishing Group 2017-03-03 /pmc/articles/PMC5335602/ /pubmed/28256624 http://dx.doi.org/10.1038/srep43727 Text en Copyright © 2017, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Huang, Renjie
Bonnichon, Arnaud
Claridge, Timothy D. W.
Leung, Ivanhoe K. H.
Protein-ligand binding affinity determination by the waterLOGSY method: An optimised approach considering ligand rebinding
title Protein-ligand binding affinity determination by the waterLOGSY method: An optimised approach considering ligand rebinding
title_full Protein-ligand binding affinity determination by the waterLOGSY method: An optimised approach considering ligand rebinding
title_fullStr Protein-ligand binding affinity determination by the waterLOGSY method: An optimised approach considering ligand rebinding
title_full_unstemmed Protein-ligand binding affinity determination by the waterLOGSY method: An optimised approach considering ligand rebinding
title_short Protein-ligand binding affinity determination by the waterLOGSY method: An optimised approach considering ligand rebinding
title_sort protein-ligand binding affinity determination by the waterlogsy method: an optimised approach considering ligand rebinding
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5335602/
https://www.ncbi.nlm.nih.gov/pubmed/28256624
http://dx.doi.org/10.1038/srep43727
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