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  • Allosteric Inhibition of the SARS-CoV-2 Main Protease: Insights from Mass Spectrometry Based Assays* #MMPMID32841477
  • El-Baba TJ; Lutomski CA; Kantsadi AL; Malla TR; John T; Mikhailov V; Bolla JR; Schofield CJ; Zitzmann N; Vakonakis I; Robinson CV
  • Angew Chem Int Ed Engl 2020[Dec]; 59 (52): 23544-23548 PMID32841477show ga
  • The SARS-CoV-2 main protease (M(pro) ) cleaves along the two viral polypeptides to release non-structural proteins required for viral replication. M(Pro) is an attractive target for antiviral therapies to combat the coronavirus-2019 disease. Here, we used native mass spectrometry to characterize the functional unit of M(pro) . Analysis of the monomer/dimer equilibria reveals a dissociation constant of Kd =0.14+/-0.03 muM, indicating M(Pro) has a strong preference to dimerize in solution. We characterized substrate turnover rates by following temporal changes in the enzyme-substrate complexes, and screened small molecules, that bind distant from the active site, for their ability to modulate activity. These compounds, including one proposed to disrupt the dimer, slow the rate of substrate processing by approximately 35 %. This information, together with analysis of the x-ray crystal structures, provides a starting point for the development of more potent molecules that allosterically regulate M(Pro) activity.
  • |*Models, Molecular[MESH]
  • |Allosteric Regulation[MESH]
  • |Binding Sites[MESH]
  • |Biological Assay[MESH]
  • |Coronavirus 3C Proteases/antagonists & inhibitors/*chemistry[MESH]
  • |Coronavirus Protease Inhibitors/*chemistry/pharmacology[MESH]
  • |Crystallography, X-Ray[MESH]
  • |Mass Spectrometry[MESH]
  • |Protein Binding[MESH]
  • |Protein Conformation[MESH]
  • |Protein Multimerization[MESH]
  • |SARS-CoV-2/*enzymology/physiology[MESH]
  • |Small Molecule Libraries/*chemistry/pharmacology[MESH]
  • |Substrate Specificity[MESH]
  • |Virus Replication[MESH]

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  • suck abstract from ncbi

    23544 52.59 2020