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Z-LRGG-AMC

Coronaviruses (CoVs) can infect humans and multiple species of animals, causing a wide spectrum of diseases. In late 2019, a novel coronavirus, termed severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) was determined as a cause for several cases of respiratory disease (Covid-19). Even though most infected patients only suffer from mild symptoms such as fever and cough associated with a good prognosis, the disease can progress into fatal cases of pneumonia and acute respiratory failure, especially in older males with comorbidities. Covid-19 rapidly spread worldwide. As of May 31st, 2022, more than 6.2 million people have died from coronavirus worldwide, and ~530 million cases have been reported. Coronavirus is a single-stranded RNA positive-strand envelope type B coronavirus. Like the other two coronaviruses that cause SARS (Severe Acute Respiratory Syndrome) and MERS (Middle East Respiratory Syndrome), SARS-CoV-2 encodes non-structural, structural, and accessory proteins. Non-structural proteins include 3-chymotrypsin-like protease (3CLpro), papain-like protease, helicase, and RNA-dependent RNA polymerase (RNA -dependent RNA polymerase (RdRp). Structural proteins include spike glycoproteins. Papain in coronavirus operates on more than 11 cleavage sites on the large polyprotein 1ab. Processing of polyproteins translated from viral RNA is essential, therefore, the main proteases are identified as an attractive drug targets for preventing virus imitation. Papain-like protease (PLpro) of coronaviruses carries out proteolytic maturation of non-structural proteins that play a role in replication of the virus and performs deubiquitination of host cell factors to scuttle antiviral responses. Z-LRGG-AMC is cleaved by papain-like proteases to give the highly fluorescent AMC product. The fluorescence intensity of released AMC is proportional to the protease activity. Z-LRGG-AMC might be used for screening and studying kinetics of PLpro inhibitors.

Spectrum

Product family

NameExcitation (nm)Emission (nm)
Z-DEVD-AMC341441
Z-KAGG-AMC341441
Z-KKAG-AMC341441

References

View all 50 references: Citation Explorer
Decoupling deISGylating and deubiquitinating activities of the MERS virus papain-like protease.
Authors: Clasman, Jozlyn R and Everett, Renata K and Srinivasan, Karthik and Mesecar, Andrew D
Journal: Antiviral research (2020): 104661
Characterization and noncovalent inhibition of the deubiquitinase and deISGylase activity of SARS-CoV-2 papain-like protease.
Authors: Freitas, Brendan T and Durie, Ian A and Murray, Jackelyn and Longo, Jaron E and Miller, Holden C and Crich, David and Hogan, Robert Jeff and Tripp, Ralph A and Pegan, Scott D
Journal: ACS infectious diseases (2020)
Structural and biochemical characterization of SADS-CoV papain-like protease 2.
Authors: Wang, Lu and Hu, Weihua and Fan, Chengpeng
Journal: Protein science : a publication of the Protein Society (2020): 1228-1241
First detection of novel enterovirus G recombining a torovirus papain-like protease gene associated with diarrhoea in swine in South Korea.
Authors: Lee, Sunhee and Lee, Changhee
Journal: Transboundary and emerging diseases (2019): 1023-1028
Identification and design of novel small molecule inhibitors against MERS-CoV papain-like protease via high-throughput screening and molecular modeling.
Authors: Lee, Hyun and Ren, Jinhong and Pesavento, Russell P and Ojeda, Isabel and Rice, Amy J and Lv, Haining and Kwon, Youngjin and Johnson, Michael E
Journal: Bioorganic & medicinal chemistry (2019): 1981-1989
Page updated on December 12, 2024

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Catalog Number13550
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Physical properties

Molecular weight

692.77

Solvent

DMSO

Spectral properties

Excitation (nm)

341

Emission (nm)

441

Storage, safety and handling

H-phraseH303, H313, H333
Hazard symbolXN
Intended useResearch Use Only (RUO)
R-phraseR20, R21, R22

Storage

Freeze (< -15 °C); Minimize light exposure
UNSPSC12171501
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