FRET peptide substrate for the severe acute respiratory syndrome coronavirus main protease (SARS-CoV Mpro). Fluorescence can be detected upon cleavage of the peptide by SARS-CoV Mpro
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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 an N-terminal a 5-carboxytetramethylrhodamine (5-TAMRA), a widely used fluorescent dye which excites at 546 nm and emits at 579 nm and a black hole quencher 2 (BHQ-2) group.
The fluorescence from 5-TAMRA is efficiently quenched by resonance energy transfer to the BHQ-2 group when the peptide is intact, however upon cleavage of the peptide by Mpro, 5-TAMRA and BHQ-2 are separated, allowing fluorescence to be detected. This therefore represents a useful tool for investigating Mpro activity.
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