Mulberrofuran G, a Potent Inhibitor of SPIKE Protein of SARS CoronaVirus ۲

Introduction: At the onset of the ۲۰۲۰ year, Coronavirus disease (COVID-۱۹) has become a pandemic and infected many people worldwide. Despite all efforts, no cure was found for this infection. Bioinformatics and medicinal chemistry have a potential role in the primary consideration of drugs to treat this infection. With virtual screening and molecular docking, some potent compounds and medications can be found and modified and then applied to treat disease in the next steps. Material and methods: By virtual screening method and PRYX software, some Food and Drug Administration(FDA) approved drugs and natural compounds have been docked with the SPIKE protein of SARSCoV-۲. Some more potent agents have been selected, and then new structures are designed with better affinity than them. After that, we searched for the molecules with a similar structure to designed compounds to find the most potent compound to our target. Results: Because of the study of structures and affinities, mulberrofuran G was the most potent compound in this study. The compound has interacted strongly with residues in the probably active site of SPIKE. Discussion: Mulberrofuran G appropriately interacts with some amino acids of SPIKE of SARS-CoV۲. These amino acids interact with human ACE ۲, too; it means these amino acids are proper residues for binding to any compound and inhibition of SPIKE of virus following that. This compound has properly binding energy for SPIKE of the virus compared to the same molecules, including some FDA-approved drugs or same designed and modified molecules, which was mentioned earlier; also there is a report of mulberrofuran G appropriate affinity to binding to ۳cl-protease of SARS corona virus ۲ ; according to these reports, mulberrofuran G can be a potent candidate for the treatment of COVID-۱۹. Conclusions: Mulberrofuran G can be a treatment agent candidate for COVID-۱۹ because of its good affinity to SPIKE of the virus and inhibition of virus-cell adhesion and entrance.