The dimer-monomer equilibrium of SARS-CoV-2 main protease is affected by small molecule inhibitors.

ABSTRACT: The maturation of coronavirus SARS-CoV-2, which is the etiological agent at the origin of the COVID-19 pandemic, requires a main protease M^pro to cleave the virus-encoded polyproteins. Despite a wealth of experimental information already available, there is wide disagreement about the M^pro monomer-dimer equilibrium dissociation constant. Since the functional unit of M^pro is a homodimer, the detailed knowledge of the thermodynamics of this equilibrium is a key piece of information for possible therapeutic intervention, with small molecules interfering with dimerization being potential broad-spectrum antiviral drug leads. In the present study, we exploit Small Angle X-ray Scattering (SAXS) to investigate the structural features of SARS-CoV-2 M^pro i

SUBMITTER: Silvestrini L 

PROVIDER: S-EPMC8085067 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature