Potential Binding Efficiency of Antiviral Drug Lopinavir Targeted to the Catalytic Dyad, His41 - Cys145 of SARS CoV -2 Main Protease
Muthu Raj S, Manohar M, Mohan M, Ganesh P, Marimuthu K
Abstract
The spread of SARS CoV 2 across the globe rushed the scientific community to find out
the potential inhibitor for controlling the viral disease. The main protease (Mpro) or
Chymotrypsin protease (3CLpro) is involved in the cleavage of polyproteins, duplication of
intracellular materials and release of nonstructural proteins. Cys-His catalytic dyad is located in
the SARS-CoV Mpro which is the substrate-binding site located in domains I and II. There are
many approved drugs that have their active protease inhibition capability. The targeting of the
active site of the main protease is the better option to fight against the viral population.
Lopinavir, ritonavir, Remdesivir and Chloroquine are some of the drug candidates considered to
be involved in the treatment of SARS CoV 2 under emergency situation as a trial basis. In the
present investigation we used lopinavir as a drug to bind the catalytic dyad His41, Cys145 of
main protease. The minimum binding of energy of -11.45 kcal/mol observed with the binding
of Cys145 and -10.93 kcal/mol was noted with the residue His41. The inhibition constant was
also found to be relevant to the binding efficiency of the drug. This is considered to be a model
drug target which is initiating the finding of many new drugs to target the current outbreak
created by the virus SARS.CoV - 2.
CORDITE (CORona Drug InTEractions database) collects and aggregates data from PubMed, MedRxiv, BioRxiv, ChemRxiv and PMC for SARS-CoV-2. Its main focus is set on drug interactions either addressing viral proteins or human proteins that could be used to treat COVID.
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