Protein-observed 19F-NMR for fragment screening, affinity quantification and druggability assessment View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2016-08

AUTHORS

Clifford T Gee, Keith E Arntson, Andrew K Urick, Neeraj K Mishra, Laura M L Hawk, Andrea J Wisniewski, William C K Pomerantz

ABSTRACT

NMR spectroscopy can be used to quantify the binding affinity between proteins and low-complexity molecules, termed 'fragments'; this versatile screening approach allows researchers to assess the druggability of new protein targets. Protein-observed (19)F-NMR (PrOF NMR) using (19)F-labeled amino acids generates relatively simple spectra that are able to provide dynamic structural information toward understanding protein folding and function. Changes in these spectra upon the addition of fragment molecules can be observed and quantified. This protocol describes the sequence-selective labeling of three proteins (the first bromodomains of Brd4 and BrdT, and the KIX domain of the CREB-binding protein) using commercially available fluorinated aromatic amino acids and fluorinated precursors as example applications of the method developed by our research group. Fragment-screening approaches are discussed, as well as Kd determination, ligand-efficiency calculations and druggability assessment, i.e., the ability to target these proteins using small-molecule ligands. Experiment times on the order of a few minutes and the simplicity of the NMR spectra obtained make this approach well-suited to the investigation of small- to medium-sized proteins, as well as the screening of multiple proteins in the same experiment. More... »

PAGES

1414-1427

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nprot.2016.079

DOI

http://dx.doi.org/10.1038/nprot.2016.079

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1002010889

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27414758


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