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

Sci Rep. 2021-04; 
Lucia Silvestrini, Norhan Belhaj, Lucia Comez, Yuri Gerelli, Antonino Lauria, Valeria Libera, Paolo Mariani, Paola Marzullo, Maria Grazia Ortore, Antonio Palumbo Piccionello, Caterina Petrillo, Lucrezia Savini, Alessandro Paciaroni, Francesco Spinozzi
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Recombinant Antibody Expression … The fluorescently labelled auto-cleavage sequence of SARS-CoV-2 M pro , ((7-Methoxycoumarin-4-yl)acetyl)-AVLQ\(\downarrow \)SGFRK(2,4-dinitrophenyl)K (purchased from GenScript), was utilized to monitor the recombinant M pro kinetics (excitation 320 nm, emission 405 … Get A Quote

摘要

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 to cleave the virus-encoded polyproteins. Despite a wealth of experimental information already available, there is wide disagreement about the M monomer-dimer equilibrium dissociation constant. Since the functional unit of M 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 fe... More

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