期刊
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
卷 12, 期 27, 页码 6252-6261出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpclett.1c01548
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资金
- National Natural Science Foundation of China [21773298]
- Key R&D Program of Zhejiang Province [2020C03010]
- Zhejiang Provincial Natural Science Foundation of China [LZ19H300001]
The study revealed that the presence of heparan sulfate is crucial for the binding between the spike protein of SARS-CoV-2 and host ACE2, while the stability of the T470-F490 loop and hydrophobic interactions play key roles in the binding process.
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection is mainly mediated through the interaction between the spike protein (S-pro) of the virus and the host angiotensin-converting enzyme II (ACE2). The attachment of heparan sulfate (HS) to S-pro is necessary for its binding to ACE2. In this study, the binding process of the receptor-binding domain (RBD) of S-pro to ACE2 was explored by enhanced sampling simulations. The free-energy landscape was characterized to elucidate the binding mechanism of S-pro to ACE2 with and without HS fragment DP4. We found that the stability of the T470-F490 loop and the hydrophobic interactions contributed from F486/Y489 in the T470-F490 loop of S-pro are quite crucial for the binding, which is enhanced by the presence of DP4. Our study provides valuable insights for rational drug design to prevent the invasion of SARS-CoV-2.
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