Antivirals are crucial for the continued control the COVID-19 pandemic and complement existing vaccine efforts. The SARS-CoV-2 main protease (Mpro) is a highly conserved functional protein that is essential for viral replication and proliferation in the host.1 With an indispensable role in the viral lifecycle and unique specificity, relative to host enzymes, Mpro is a very attractive target for the development of antiviral therapeutics to combat the COVID-19 pandemic.1-3 Indeed, Nirmatrelvir (Pfizer), the first antiviral approved for clinical use that was specifically designed for the SARS-CoV-2 virus, inhibits Mpro.
With a view to developing highly potent and selective antiviral targeting SARS-CoV-2 Mpro we performed Random nonstandard Peptide Integrated Discovery (RaPID) mRNA display against a chemically-cross linked SARS-CoV-2 Mpro dimer. This led to the discovery of several potent thioether-linked cyclic peptide inhibitors of the target in vitro.4-7 Structural analysis of the Mpro complexed with a selenoether analogue of the most potent inhibitor revealed fundamental binding interactions responsible for activity; a glutamine and leucine residue in the S1 and S2 sites respectively, in concert with a binding configuration that straddles both chains of the physiological dimer. The structure-activity relationships that characterise the lead Mpro inhibitor were probed with a series of alanine analogues that further complemented these findings. When assessed in vivo, several of the Mpro inhibitors exhibited antiviral activity against SARS-CoV-2 with EC50 values in the low micromolar range that could be enhanced further with the appendage of a cell-penetrating peptide. Collectively, these cyclic peptide Mpro inhibitors provide a promising foundation for the development of antiviral therapeutics specific to SARS-CoV-2.