Rydzik Anna M, Brem Jürgen, Chandler Shane A, Benesch Justin L P, Claridge Timothy D W, Schofield Christopher J
The Department of Chemistry , University of Oxford , 12 Mansfield Road , Oxford , OX1 3TA , UK . Email:
RSC Med Chem. 2020 Feb 21;11(3):387-391. doi: 10.1039/c9md00416e. eCollection 2020 Mar 1.
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.
利用新德里金属β-内酰胺酶1，对氟核磁共振蛋白质观测光谱法作为一种分析蛋白质金属结合的方法进行了评估。结果表明，氟核磁共振对于分析不同金属化的蛋白质状态以及研究抑制剂存在时的平衡状态很有用。一个局限性是氟标记可能会影响金属离子结合。氟核磁共振光谱所观测到的蛋白质行为变化的灵敏读出，再加上广泛的耐受条件范围（缓冲液变化），意味着在药物研发过程中，对于研究金属离子相互作用以及金属酶的抑制作用，应进一步研究氟核磁共振。
