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

• Published in: RSC medicinal chemistry Vol. 11; no. 3; pp. 387 - 391
• Main Authors: Rydzik, Anna M, Brem, Jürgen, Chandler, Shane A, Benesch, Justin L P, Claridge, Timothy D W, Schofield, Christopher J
• Format: Journal Article
• Language: English
• Published: England 30-03-2020
• ISSN: 2632-8682; 2632-8682
• DOI: 10.1039/C9MD00416E

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
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
F labelling may affect metal ion binding. The sensitive readout of changes in protein behaviour observed by
F NMR spectra coupled with the broad scope of tolerated conditions (
buffer variations) means
F NMR should be further investigated for studying metal ion interactions and the inhibition of metallo-enzymes during drug discovery.