Search results for " main protease Mpro"

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

2021

AbstractThe maturation of coronavirus SARS-CoV-2, which is the etiological agent at the origin of the COVID-19 pandemic, requires a main protease Mpro to cleave the virus-encoded polyproteins. Despite a wealth of experimental information already available, there is wide disagreement about the Mpro monomer-dimer equilibrium dissociation constant. Since the functional unit of Mpro 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 (…

0301 basic medicineMolecular biologyProtein ConformationSciencemedicine.medical_treatmentDimerBiophysicsPlasma protein binding010402 general chemistryAntiviral Agents01 natural sciencesArticleDissociation (chemistry)03 medical and health scienceschemistry.chemical_compoundProtein structureX-Ray DiffractionDrug DiscoverymedicineHumansProtease InhibitorsCoronavirus 3C ProteasesVirtual screeningMultidisciplinaryProteaseSARS-CoV-2ChemistryQSARS-CoV-2 main protease Mpro enzymatic activity inhibition Small Angle X-ray Scattering small inhibitors virtual screeningRCOVID-19Computational BiologySmall moleculeComputational biology and bioinformatics0104 chemical sciencesMolecular Docking SimulationDissociation constant030104 developmental biologyBiophysicsMedicineThermodynamicsDimerizationProtein Binding
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