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Results for "

polyproteins

" in MedChemExpress (MCE) Product Catalog:

5

Inhibitors & Agonists

1

Fluorescent Dye

3

Peptides

1

Natural
Products

Cat. No. Product Name Target Research Areas Chemical Structure
  • HY-P4039
    Ac-EEVVAC-pNA

    		HCV Protease Infection
    Ac-EEVVAC-pNA is a chromogenic substrate for a continuous spectrophotometric assay of HCV NS3 protease. The sequence EEVVAC is derived from the 5A-5B cleavage junction of the HCV polyprotein .
    Ac-EEVVAC-pNA
  • HY-152222
    SPR38

    		SARS-CoV Cathepsin Infection
    SPR38 is a potent SARS-CoV-2 main protease inhibitor, with a Ki of 0.260 μM. SPR38 also inhibits hCatL and hCatB, with Ki values of 1.92 μM and 11.1 μM, respectively .
    SPR38
  • HY-E70018
    Picornain 3C

    		Endogenous Metabolite Infection Metabolic Disease
    Picornain 3C is a protease found in picornaviruses, which cleaves peptide bonds of non-terminal sequences. Picornain 3C is an intermediate between the serine peptidase chymotrypsin and the cysteine peptidase papain. Picornain 3C shows endopeptidase activity by selectively cleaving Gln-Gly bonds in the polyprotein of poliovirus and with substitution of Glu for Gln, and Ser or Thr for Gly in other picornaviruses .
    Picornain 3C
  • HY-N144101
    SARS-CoV MPro-IN-2

    		SARS-CoV Infection
    SARS-CoV MPro-IN-2 (compound 15) is a potent inhibitor of SARS-CoV-2 M pro with an IC50 value of 72.07 nM. The main protease (M pro) of the virus as the major enzyme processing viral polyproteins contributes to the replication and transcription of SARS-CoV-2 in host cells, and has been characterized as an attractive target in agent discovery. SARS-CoV MPro-IN-2 has the potential for the research of COVID-19 .
    SARS-CoV MPro-IN-2
  • HY-117747
    DMP 323

    JCR 424; XM 323

    		 HIV Protease Infection
    DMP 323 is a potent, nonpeptide cyclic urea inhibitor of HIV protease, effective against both HIV type 1 and type 2. Designed using structural information and database searching, it competitively inhibits the cleavage of both peptide and HIV-1 gag polyprotein substrates. DMP 323 shows comparable potency to other highly effective HIV protease inhibitors like A-80987 and Ro-31-8959. Importantly, its efficacy against HIV protease remains unaffected by human plasma or serum, suggesting low affinity for plasma proteins. Furthermore, DMP 323 demonstrates minimal inhibition of various mammalian proteases at concentrations much higher than those needed for HIV protease inhibition, highlighting its specificity for viral targets .
    DMP 323

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