2. Search Result
Search Result
Results for "

viral polyproteins

" in MedChemExpress (MCE) Product Catalog:

7

Inhibitors & Agonists

2

Peptides

2

Natural
Products

Cat. No. Product Name Target Research Areas Chemical Structure
  • HY-N15365
    Antcin B

    		Virus Protease SARS-CoV Infection
    Antcin B is a SARS-CoV-2 3-chymotrypsin-like protease (3CL Pro) inhibitor. Antcin B binds to multiple key amino acid residues of 3CL Pro(such as Leu141, Asn142, Glu166, His163, etc.) through hydrogen bonds, salt bridges, and hydrophobic interactions, thereby inhibiting the activity of 3CL Pro, blocking the cleavage process of viral polyproteins, and suppressing the replication of the SARS-CoV-2 virus in host cells. Antcin B is promising for research of COVID-19 .
    Antcin B
  • HY-P5505
    LCMV-derived p13 epitope

    		Arenavirus Others
    LCMV-derived p13 epitope is a biological active peptide. (An H-2Db restricted epitope, this peptide is amino acids 61 to 80 fragment of the lymphocytic choriomeningitis virus (LCMV) pre-glycoprotein polyprotein GP complex. LCMV has been routinely used for the study of adaptive immune responses to viral infection.)
    LCMV-derived p13 epitope
  • 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-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-159911
    SARS-CoV-2 Mpro-IN-29

    		SARS-CoV Virus Protease
    SARS-CoV-2 Mpro-IN-29 (Compound 7) is an inhibitor of the SARS-CoV-2 main protease (Mpro) with an IC50 of 310 nM and an EC50 of 0.5 μM in Vero cells. SARS-CoV-2 Mpro-IN-29 binds to the active site of Mpro, blocking the cleavage of viral polyproteins, showing significant antiviral activity and enhanced metabolic function. SARS-CoV-2 Mpro-IN-29 holds potential for research on SARS-CoV-2 antiviral agents .
    SARS-CoV-2 Mpro-IN-29
  • 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
  • HY-P5415
    DABCYL-GABA-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln-EDANS

    		HIV Others
    DABCYL-GABA-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln-EDANS is a biological active peptide. (DABCYL-GABA-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln-EDANS is also called HIV protease substrate I in some literature. It is widely used for the continuous assay for HIV protease activity. The 11-kD protease (PR) encoded by the human immunodeficiency virus 1 (HIV-1) is essential for the correct processing of viral polyproteins and the maturation of infectious virus, and is therefore a target for the design of selective acquired immunodeficiency syndrome (AIDS) therapeutics. The FRET-based fluorogenic substrate is derived from a natural processing site for HIV-1 PR. Incubation of recombinant HIV-1 PR with the fluorogenic substrate resulted in specific cleavage at the Tyr-Pro bond and a time-dependent increase in fluorescence intensity that is linearly related to the extent of substrate hydrolysis. The fluorescence quantum yields of the HIV-1 PR substrate in the FRET assay increased by 40.0- and 34.4-fold, respectively, per mole of substrate cleaved. Because of its simplicity and precision in the determination of reaction rates required for kinetic analysis, this substrate offers many advantages over the commonly used HPLC or electrophoresis-based assays for peptide substrate hydrolysis by retroviral PRs. Abs/Em = 340nm/490nm.)
    DABCYL-GABA-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln-EDANS

Inquiry Online

Your information is safe with us. * Required Fields.

Salutation

  

Country or Region *

Applicant Name *

 

Organization Name *

Department *

     

Email Address *

 

Product Name *

Cat. No.

  

Requested quantity *

Phone Number *

     

Remarks

Inquiry Online

Inquiry Information

Product Name:
Cat. No.:
Quantity:
MCE Japan Authorized Agent: