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Fluorescent substrate for Furin protease

Specifications

Sequence: Pyr-Arg-Thr-Lys-Arg-AMC (AMC = 7-Amino-4-methylcoumarin).

Molecular Mass: 827.94 Da.

Purity: > 95% based on HPLC.

Quantity: 5 x 200 mg lyophilized powder


Assay Conditions
A fluorescence plate reader with excitation at 380 nm and emission at 460 nm is recommended for
the measurement of the enzymatic activity. Depending upon individual enzymes, the substrate can
be used at final concentrations between 10 - 100 µM in a total of 100 µL reaction mixture.

Applications
Hydrolysis of Arg-AMC amide bond releases AMC, a highly fluorescent group.
It is an excellent substrate for furin-like proprotein convertases


MESH: Human Furin , West Nile Virus NS3 Protease

References:

K. Hatsuzawa, M. Nagahama, S. Takahashi, K. Takada, K. Murakami and K. Nakayama, J. Biol. Chem., 267, 16094 (1992)

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Reference

Furin‐mediated protein processing in infectious diseases and cancer

Elisabeth Braun 1 and Daniel Sauter 1

Viruses. 2019 Oct 31;11(11). pii: E1011. doi: 10.3390/v11111011.

Decanoyl-Arg-Val-Lys-Arg-Chloromethylketone: An Antiviral Compound That Acts against Flaviviruses through the Inhibition of Furin-Mediated prM Cleavage.
Imran M1,2,3,4, Saleemi MK5, Chen Z6,7,8, Wang X9,10,11, Zhou D12,13,14, Li Y15,16,17, Zhao Z18,19,20, Zheng B21,22,23, Li Q24,25,26, Cao S27,28,29, Ye J30,31,32.


Abstract
Flaviviruses, such as Zika virus (ZIKV), Japanese encephalitis virus (JEV), Dengue virus (DENV), and West Nile virus (WNV), are important arthropod-borne pathogens that present an immense global health problem. Their unpredictable disease severity, unusual clinical features, and severe neurological manifestations underscore an urgent need for antiviral interventions. Furin, a host proprotein convertase, is a key contender in processing flavivirus prM protein to M protein, turning the inert virus to an infectious particle. For this reason, the current study was planned to evaluate the antiviral activity of decanoyl-Arg-Val-Lys-Arg-chloromethylketone, a specific furin inhibitor, against flaviviruses, including ZIKV and JEV. Analysis of viral proteins revealed a significant increase in the prM/E index of ZIKV or JEV in dec-RVKR-cmk-treated Vero cells compared to DMSO-treated control cells, indicating dec-RVKR-cmk inhibits prM cleavage. Plaque assay, qRT-PCR, and immunofluorescence assay revealed a strong antiviral activity of dec-RVKR-cmk against ZIKV and JEV in terms of the reduction in virus progeny titer and in viral RNA and protein production in both mammalian cells and mosquito cells. Time-of-drug addition assay revealed that the maximum reduction of virus titer was observed in post-infection treatment. Furthermore, our results showed that dec-RVKR-cmk exerts its inhibitory action on the virus release and next round infectivity but not on viral RNA replication. Taken together, our study highlights an interesting antiviral activity of dec-RVKR-cmk against flaviviruses.
KEYWORDS:
Japanese encephalitis virus; Zika virus; flavivirus; furin inhibitor; precursor membrane protein
PMID: 31683742 PMCID: PMC6893617 DOI: 10.3390/v11111011
Free PMC Article

https://www.ncbi.nlm.nih.gov/pubmed/31683742

Leitsubstanz / Leitstruktur
COVID - ACE2 Entry Inhibitor

Leitsubstanz: YKYRYL
(Y438 - L443)
Wirksam im quantitativen RT-PCR Assay:
Kompetitive Inhibition der Virusproliferation in VeroE6 Zellen.
Wirksam im Bereich ab 7-10 mM

Zugriffe heute: 1 - gesamt: 947.

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