新型噻二唑烷酮衍生物对 SARS-CoV-2 主要蛋白酶的分子相互作用和抑制作用
Molecular interactions and inhibition of the SARS-CoV-2 main protease by a thiadiazolidinone derivative.
机构信息
Department of Chemical Engineering, University of New Hampshire, Durham, New Hampshire, USA.
Department of Molecular, Cellular, and Biomedical Services, University of New Hampshire, Durham, New Hampshire, USA.
出版信息
Proteins. 2022 Nov;90(11):1896-1907. doi: 10.1002/prot.26385. Epub 2022 Jun 3.
We report molecular interactions and inhibition of the main protease (M ) 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 via docking protocols and molecular dynamics simulations in all-atom detail. We reveal the local and global dynamics of M in the presence of this inhibitor and confirm the inhibition of the enzyme with an IC value of 1.39 ± 0.22 μM, which is comparable to other known inhibitors of this enzyme.
我们报告了 SARS-CoV-2 的主要蛋白酶（M ）的分子相互作用和抑制，该酶是病毒生命周期中涉及的关键酶。我们使用噻二唑烷酮（TDZD）衍生物作为化学探针，通过对接方案和全原子细节的分子动力学模拟来探索 M 的构象动力学。我们揭示了在存在这种抑制剂的情况下 M 的局部和整体动力学，并证实了该酶的抑制作用，其 IC 值为 1.39±0.22μM，与该酶的其他已知抑制剂相当。
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