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Monitoring protein-metal binding by (19)F NMR – a case study with the New Delhi metallo-β-lactamase 1

(19)F NMR protein observed spectroscopy is evaluated as a method for analysing protein metal binding using the New Delhi metallo-β-lactamase 1. The results imply (19)F NMR is useful for analysis of different metallated protein states and investigations on equilibrium states in the presence of inhibi...

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Detalles Bibliográficos
Autores principales: Rydzik, Anna M., Brem, Jürgen, Chandler, Shane A., Benesch, Justin L. P., Claridge, Timothy D. W., Schofield, Christopher J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7484990/
https://www.ncbi.nlm.nih.gov/pubmed/33479644
http://dx.doi.org/10.1039/c9md00416e
Descripción
Sumario:(19)F NMR protein observed spectroscopy is evaluated as a method for analysing protein metal binding using the New Delhi metallo-β-lactamase 1. The results imply (19)F NMR is useful for analysis of different metallated protein states and investigations on equilibrium states in the presence of inhibitors. One limitation is that (19)F labelling may affect metal ion binding. The sensitive readout of changes in protein behaviour observed by (19)F NMR spectra coupled with the broad scope of tolerated conditions (e.g. buffer variations) means (19)F NMR should be further investigated for studying metal ion interactions and the inhibition of metallo-enzymes during drug discovery.