Abstract
A commentary on the article by Luchinat et al. [(2021), Acta Cryst. D77, 1247–1258] where they describe an approach to identify the details of a compound binding to a molecular target using in-cell NMR to provide intracellular binding affinities.
Highlights
The real-time nuclear magnetic resonance (NMR) bioreactor setup described promises to be well suited to obtain comprehensive and time-resolved datasets for cellular compound uptake and, at the same time, intracellular compound–target interactions
Whereas it still remains to be shown whether this approach can be applied to other target proteins, these findings promise that in-cell NMR can provide a new route to the determination of intracellular ligand-binding affinities for other target proteins in the future
This approach should be applicable to all target proteins provided that (i) they can be expressed or introduced in cells isotopically labeled at sufficient concentrations (>10 mM); (ii) there is a lack of binding to other cellular components which would cause extensive broadening of NMR signals; (iii) there is sufficient protein stability; (iv) there are well separated NMR signals in the cellular background; (v) sufficient chemical shift differences are induced by ligand-binding and (iv) there is strong ligand binding
Summary
The real-time NMR bioreactor setup described promises to be well suited to obtain comprehensive and time-resolved datasets for cellular compound uptake and, at the same time, intracellular compound–target interactions. Whereas it still remains to be shown whether this approach can be applied to other target proteins, these findings promise that in-cell NMR can provide a new route to the determination of intracellular ligand-binding affinities for other target proteins in the future.
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