ArgRS Inhibitors

Arginyl-tRNA synthetase (ArgRS) is an indispensable cog in the machinery of protein synthesis, facilitating the proper charging of tRNA with the amino acid arginine. As such, the correct functioning of ArgRS and its related enzymes is a critical step in cellular protein translation. Given its importance, a disruption in the activity of ArgRS can effectively stall protein synthesis. Borrelidin is one of the compounds recognized to inhibit several aminoacyl-tRNA synthetases, including ArgRS. Mupirocin, another inhibitor, although primarily acting against isoleucyl-tRNA synthetase, can cast a broader inhibitory net across the aminoacyl-tRNA synthetase family.

Similarly, agents like Cladosporin and Indolmycin, while having primary targets such as lysyl-tRNA and tryptophanyl-tRNA synthetases, respectively, can indirectly influence the functioning of ArgRS. Halofuginone and Relacin further showcase the breadth of inhibition across this enzyme family. The synthetic compound AN2690, known to primarily target fungal leucyl-tRNA synthetase, might have wider-ranging effects on other tRNA synthetases. Cefiderocol, with its ability to chelate iron, can interfere with the metal-assisted operations of certain enzymes, thereby having an indirect impact on ArgRS. Tavaborole, Blasticidin S, L-Histidinol, and aminoacyl adenylate analogs further extend the list of compounds that, while not directly targeting ArgRS, can influence its activity and the broader landscape of aminoacyl-tRNA synthetase family.