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nsp12 polymerase inhibitor

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Cat. No. Product Name Target Research Areas Chemical Structure
  • HY-174439

    SARS-CoV Virus Protease Drug Metabolite Infection
    Nsp12-IN-2 (Compound 8), the triphosphate metabolite of 4'-thiouridine (HY-W113081), is a SARS-CoV-2 Nsp12 inhibitor. Nsp12-IN-2 inhibits the RNA-dependent RNA polymerase (RdRp) activity of the SARS-CoV-2 Nsp12-Nsp7-Nsp8 complex, terminates RNA synthesis and also blocks the RNAylation and NMPylation of Nsp9. Nsp12-IN-2 is promising for research of infections caused by SARS-CoV-2, other coronaviruses, and other RNA viruses .
    Nsp12-IN-2
  • HY-N14351

    SARS-CoV Bacterial Antibiotic Infection
    Ferrocin A is a lipopeptide compound that targets the SARS-CoV-2 RNA-dependent RNA polymerase (nsp12). Ferrocin A can stably bind to nsp12, and as an iron-chelating peptide, it reduces the concentration of free iron in the environment via complexation, thereby inhibiting bacterial growth by repressing the acquisition of essential metal cations. As an iron-chelating antiviral molecule, Ferrocin A may be used in studies related to COVID-19 and bacterial infections .
    Ferrocin A
  • HY-158322

    SARS-CoV Infection
    Nsp12-IN-1 is a nucleoside analogue. Nsp12-IN-1 can block the synthesis of viral RNA and inhibit viral replication. Nsp12-IN-1 can be used in the study of pan-coronavirus .
    nsp12-IN-1
  • HY-181778

    SARS-CoV DNA/RNA Synthesis Infection
    RdRP-IN-10 is a SARS-CoV-2 RNA-dependent RNA polymerase (RdRp) inhibitor with an IC50 value of 5.78 μM. RdRP-IN-10 forms covalent binds with SARS-CoV-2 nsp8 Cys114, disrupts nsp8-nsp12 stabilizing interactions. RdRP-IN-10 inhibits SARS-CoV-2 RdRp-mediated RNA polymerization without interfering with RNA-RdRp complex binding. RdRP-IN-10 exerts antiviral effects in cellular models. RdRP-IN-10 can be used for the research of SARS-CoV-2 infection .
    RdRP-IN-10

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