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SARS-CoV-2 main protease Mpro (3CLpro) represents a major target in drug development against COVID-19. Prior to cleavage, rhodamine is bound to glutamine and thus not fluorescent. Upon cleavage, the fluorophore becomes active. This rhodamine 110 based Mpro substrate has a red-shifted excitation (492 nm) and emission (529) compared to the FRET substrate LS-4180. It shows a better signal-to-noise ratio and produces less interference with potential inhibitors in screening assays. This leads to a higher sensitivity compared to the Dabcyl/Edans substrate. In consequence, lower substrate amounts are required for successful assays. Dissolve in dry DMSO and use as aliquots.
α-Ketoamides as Broad-Spectrum Inhibitors of Coronavirus and Enterovirus Replication: Structure-Based Design, Synthesis, and Activity Assessment; L. Zhang, D. Lin, Y. Kusov, Y. Nian, Q. Ma, J. Wang, A. von Brunn, P. Leyssen, K. Lanko, J. Neyts, A. de Wilde, E. J. Snijder, H. Liu, and R. Hilgenfeld; J. Med. Chem. 2020; 63: 4562-4578; https://doi.org/10.1021/acs.jmedchem.9b01828
A structural view of the inactivation of the SARS coronavirus main proteinase by benzotriazole esters; K. H. G. Verschueren, K. Pumpor, S. Anemüller, S. Chen, J. R. Mesters, R. Hilgenfeld; Chem. Biol. 2008; 15: 597-606; https://doi.org/10.1016/j.chembiol.2008.04.011.
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