期刊
CHEMBIOCHEM
卷 22, 期 5, 页码 865-875出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.202000455
关键词
COVID-19; free energy of binding; molecular docking; molecular dynamics; spike protein
资金
- CNPq
- Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior - Brasil (CAPES) [001]
The higher chemical affinity of SARS-CoV-2 for hACE2 compared to SARS-CoV makes it more difficult to treat SARS-CoV-2 with drugs targeting its spike protein. This research helps to explain the infectivity of SARS-CoV-2.
The SARS-CoV-2 pandemic is the biggest health concern today, but until now there is no treatment. One possible drug target is the receptor binding domain (RBD) of the coronavirus' spike protein, which recognizes the human angiotensin-converting enzyme 2 (hACE2). Our in silico study discusses crucial structural and thermodynamic aspects of the interactions involving RBDs from the SARS-CoV and SARS-CoV-2 with the hACE2. Molecular docking and molecular dynamics simulations explain why the chemical affinity of the new SARS-CoV-2 for hACE2 is much higher than in the case of SARS-CoV, revealing an intricate pattern of hydrogen bonds and hydrophobic interactions and estimating a free energy of binding, which is consistently much more negative in the case of SARS-CoV-2. This work presents a chemical reason for the difficulty in treating the SARS-CoV-2 virus with drugs targeting its spike protein and helps to explain its infectiousness.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据