RBD-ACE2 binding properties in five SARS-CoV-2 variants of concern with new perspectives in the design of pan-coronavirus peptide inhibitors - 28/01/23
Doi : 10.1016/j.jinf.2022.09.011
Fangfang Yan a, Feng Gao a, b, c, ⁎ 
a Department of Physics, School of Science, Tianjin University, Tianjin 300072, China
b Frontiers Science Center for Synthetic Biology and Key Laboratory of Systems Bioengineering (Ministry of Education), Tianjin University, Tianjin 300072, China
c SynBio Research Platform, Collaborative Innovation Center of Chemical Science and Engineering (Tianjin), Tianjin 300072, China
⁎Corresponding author at: Department of Physics, School of Science, Tianjin University, Tianjin, China.Department of PhysicsSchool of ScienceTianjin UniversityTianjinChina
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Highlights |
• | Mutations occurring in five SARS-CoV-2 variants resulted in obvious changes in the correlation network of residues. |
• | Compared with the original strain, the binding affinity of five variants to ACE2 was strengthened. |
• | The driving force for the preferential binding of five variants to ACE2 was identified. |
• | Those key residues responsible for the enhanced receptor-binding ability of variants were identified. |
• | The peptide inhibitor designed in this study can stably bind to all investigated SARS-CoV-2 strains. |
Abbreviations : VOCs, ACE2, MD, RBDs
© 2022
Publié par Elsevier Masson SAS.
Vol 86 - N° 2
P. e51-e54 - février 2023 Retour au numéro
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