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Yang et al (2005) Design of Wide-Spectrum Inhibitors Targeting Coronavirus Main Proteases. PLoS Biol. 3(10) e324 www.ncbi.nlm.nih.gov/pubmed/16128623
Zhao et al (2008). Structure of the Main Protease from a Global Infectious Human Coronavirus, HCoV-HKU1. J. Virol. 82(17) 8647 www.ncbi.nlm.nih.gov/pubmed/18562531
Fluorescently labelled substrate for the severe acute respiratory syndrome coronavirus main protease (SARS-CoV Mpro). The substrate sequence is derived from residues P4–P5' of the SARS-CoV Mpro N-terminal autoprocessing site which has the sequence AVLQSGFRK. SARS-CoV Mpro is a key antiviral target.
This peptide contains a highly fluorescent N-terminal 7-methoxycoumarin fluorophore (Mca) and a 2,4-dinitrophenyl (Dnp) quencher. Mca is efficiently quenched by resonance energy transfer to the 2,4-dinitrophenyl group when the peptide is intact, however upon cleavage of the peptide by Mpro, the Mca group and the Dnp quencher are separated and fluorescence can be detected. This therefore represents a useful tool for investigating Mpro activity.
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