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The transforming growth factor beta-receptor I/activin receptor-like kinase 5 (TGFBR1/ALK5) and its close homologue ALK4 are receptor protein kinases associated with the development of diverse diseases, including cancer, fibrosis, heart diseases, and dysfunctional immune response. Therefore, ALK4/5 are among the most studied kinases, and several inhibitors have been developed. However, current commercially available inhibitors either lack selectivity or have not been comprehensively characterized, limiting their value for studying ALK4/5 function in cellular systems. To this end, we report the characterization of the 2-oxo-imidazopyridine, TP-008, a potent chemical probe with dual activity for ALK4 and ALK5 as well as the development of a matching negative control compound. TP-008 has excellent cellular potency and strongly abrogates phosphorylation of the substrate SMAD2 (mothers against decapentaplegic homologue 2). Thus, this chemical probe offers an excellent tool for mechanistic studies on the ALK4/5 signaling pathway and the contribution of these targets to disease.

Original publication

DOI

10.1021/acschembio.0c00076

Type

Journal article

Journal

ACS Chem Biol

Publication Date

17/04/2020

Volume

15

Pages

862 - 870

Keywords

Activin Receptors, Type I, Animals, Binding Sites, HEK293 Cells, Humans, Imidazoles, Mice, Molecular Docking Simulation, Phosphorylation, Protein Binding, Protein Kinase Inhibitors, Pyridines, Receptor, Transforming Growth Factor-beta Type I, Signal Transduction, Smad2 Protein