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Article Dans Une Revue Journal of the American Chemical Society Année : 2012

Boosting Sensitivity of Ligand-Protein Screening by NMR of Long-Lived States.

Résumé

A new NMR method for the study of ligand-protein interactions by NMR exploits the unusual lifetimes of long-lived states (LLS). The new method provides better contrast between bound and free ligands, and requires a protein-ligand ratio about 25 times lower than established T1ρ methods, thus saving on costly proteins. The new LLS method was applied to the screening of inhibitors of urokinase-type plasminogen activator (uPA), which is a prototypical target of cancer research. Using only 10 μM protein, a dissociation constant KD = 180 +/- 20 nM has been determined for the strong ligand (inhibitor) UK-18, which can be compared with KD = 157 +/- 39 nM determined by the established SPR method.

Domaines

Chimie organique

Dates et versions

hal-00710084 , version 1 (20-06-2012)

Identifiants

Citer

Nicola Salvi, Roberto Buratto, Aurélien Bornet, Simone Ulzega, Inmaculada Rentero Rebollo, et al.. Boosting Sensitivity of Ligand-Protein Screening by NMR of Long-Lived States.. Journal of the American Chemical Society, 2012, 134 (27), pp.11076-11079. ⟨10.1021/ja303301w⟩. ⟨hal-00710084⟩
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