Abstract
We report molecular interactions and inhibition of the main protease (M Pro ) of SARS-CoV-2, a key enzyme involved in the viral life cycle. By using a thiadiazolidinone (TDZD) derivative as a chemical probe, we explore the conformational dynamics of M Pro via docking protocols and molecular dynamics simulations in all-atom detail. We reveal the local and global dynamics of M Pro in the presence of this inhibitor and confirm the inhibition of the enzyme with an IC 50 value of 1.39 ± 0.22 μM, which is comparable to other known inhibitors of this enzyme.
Keywords: SARS-CoV-2; docking; main protease; molecular dynamics; thiadiazolidinone.
All Keywords
【저자키워드】 SARS-CoV-2, main protease, docking, molecular dynamics, thiadiazolidinone., 【초록키워드】 protocol, Local, protease, Molecular dynamics simulation, molecular, inhibitor, enzyme, viral life cycle, molecular interaction, probe, involved, conformational, comparable, Pro, 【제목키워드】 protease, Interaction, the SARS-CoV-2,
【저자키워드】 SARS-CoV-2, main protease, docking, molecular dynamics, thiadiazolidinone., 【초록키워드】 protocol, Local, protease, Molecular dynamics simulation, molecular, inhibitor, enzyme, viral life cycle, molecular interaction, probe, involved, conformational, comparable, Pro, 【제목키워드】 protease, Interaction, the SARS-CoV-2,