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ACS Comb Sci. Targeting the dimerization of main protease of coronaviruses: A potential broad-spectrum therapeutic strategy

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  • ACS Comb Sci. Targeting the dimerization of main protease of coronaviruses: A potential broad-spectrum therapeutic strategy


    ACS Comb Sci. 2020 May 13. doi: 10.1021/acscombsci.0c00058. [Epub ahead of print]
    Targeting the dimerization of main protease of coronaviruses: A potential broad-spectrum therapeutic strategy.


    Goyal B, Goyal D.

    Abstract

    A new coronavirus (CoV) caused a pandemic COVID-19, which has become a global health care emergency in the present date. The virus has been termed as SARS-CoV-2 (Severe Acute Respiratory Syndrome-Cororavirus-2) and has a genome similar (~82%) to the SARS-CoV (SARS coronavirus). An attractive therapeutic target for CoVs is the Mpro (main protease) or 3CLpro (3-chymotrypsin-like cysteine protease) as the enzyme plays a key role in the polyprotein processing and is active in a dimeric form. Further, Mpro is highly conserved among various CoVs as the mutation in Mpro is often lethal to the virus. Thus, drugs targeting Mpro enzyme significantly reduce the risk of mutation-mediated drug resistance and display broad-spectrum antiviral activity. The combinatorial design of peptide-based inhibitors targeting the dimerization of SARS-CoV Mpro represent a potential therapeutic strategy. In this regard, we compiled the literature reports highlighting the effect of mutations and N-terminal deletion of residues of SARS-CoV Mpro on its dimerization and thus, catalytic activity. We believe that the present review will stimulate research in this less explored, yet quite significant area. The effect of the COVID-19 epidemic and the possibility of future CoV outbreaks strongly emphasize the urgent need for the design and development of potent antiviral agents against CoV infections.



    PMID:32402186DOI:10.1021/acscombsci.0c00058


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