Benchmarking the ability of novel compounds to inhibit SARS-CoV-2 main protease using steered molecular dynamics simulations.

ABSTRACT:

Background

The SARS-CoV-2 main protease (M^pro) is an attractive target in the COVID-19 drug development process. It catalyzes the polyprotein's translation from viral RNA and specifies a particular cleavage site. Due to the absence of identical cleavage specificity in human cell proteases, targeting M^pro with chemical compounds can obstruct the replication of the virus.

Methods

To explore the potential binding mechanisms of 1,2,3-triazole scaffolds in comparison to co-crystallized inhibitors 11a and 11b towards M^pro, we herein utilized molecular dynamics and enhanced sampling simulation studies.

Results and conclusion

All the 1,2,3-triazole scaffolds interacted with catalytic residues (Cys145 and His41) and binding pocket residues of M

SUBMITTER: Singh R 

PROVIDER: S-EPMC9052739 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature