The new type of coronavirus, SARS-CoV-2 has affected more than 22.6 million people worldwide. Since the first day the virus was spotted in Wuhan, China, numerous drug design studies have been conducted all over the globe. Most of these studies target the receptor-binding domain of spike protein of SARS-CoV-2, which is known to bind to the human ACE2 receptor and SARS-CoV-2 main protease, vital for the virus’ replication. However, there might be a third target, human furin protease, which cleaves the virus’ S1-S2 domains playing an active role in its entry into the host cell. In this study, we docked five clinically used drug molecules, favipiravir, hydroxychloroquine, remdesivir, lopinavir, and ritonavir onto three target proteins, the receptor-binding domain of SARS-CoV-2 spike protein, SARS-CoV-2 main protease, and human furin protease. Results of molecular docking simulations revealed that human furin protease might be targeted by COVID-19. Remdesivir, a nucleic acid derivative, strongly bound to the active site of this protease, suggesting that this molecule can be used as a template for designing novel furin protease inhibitors to fight against the disease. Protein-drug interactions revealed in this study at the molecular level, can pave the way for better drug design for each specific target.
【저자키워드】 COVID-19, SARS-CoV-2, molecular docking, Remdesivir, furin protease, 【초록키워드】 coronavirus, Hydroxychloroquine, drug design, Ritonavir, Favipiravir, protease, virus, SARS-CoV-2 main protease, Spike protein, Replication, nucleic acid, SARS-CoV-2 spike protein, molecular, inhibitor, Interaction, host cell, domain, human ACE2 receptor, target proteins, MOST, FIVE, Wuhan, China, Result, affected, globe, clinically, the disease, conducted, can be used, the receptor-binding domain, cleave, docked, 【제목키워드】 clinically, approved, SARS-CoV-2 drug,