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- W4387661567 abstract "The SARS-CoV-2 main protease (Mpro ) holds significant importance as a biological target in combating coronaviruses due to its importance in virus replication. Considering the emergence of novel SARS-CoV-2 variants and the mutations observed in the Mpro sequence, we hypothesized that these mutations may have a potential impact on the protease's specificity. To test this, we expressed Mpro corresponding to the original strain and variants Beta1, Beta2 and Omicron, and analyzed their activity on protein-based and peptide substrates. Although we observed differential activity on the protein-based substrate, there was very little difference when analyzed on the peptide substrate. We conclude that mutations on the Mpro sequence, despite having a minor effect on a peptide substrate cleavage, did not change the catalytic site environment enough to build resistance to inhibition. Therefore, we propose that inhibitors initially designed for the Mpro of the original strain will be effective in all the variants. Thus, Mpro is likely to continue to be a target of therapeutic interest as mutations in its sequence are rare and, as we show here, have a minor effect on the protease's recognition of peptide-based molecules." @default.
- W4387661567 created "2023-10-17" @default.
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- W4387661567 date "2023-10-16" @default.
- W4387661567 modified "2023-10-17" @default.
- W4387661567 title "Differential specificity of SARS‐CoV‐2 main protease variants on peptide versus protein‐based substrates" @default.
- W4387661567 doi "https://doi.org/10.1111/febs.16970" @default.
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- W4387661567 hasPublicationYear "2023" @default.
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