6533b7d2fe1ef96bd125f8ce
RESEARCH PRODUCT
Thermodynamic analysis of the interactions between human ACE2 and spike RBD of Betacoronaviruses (SARS-CoV-1 and SARS-CoV-2)
subject
binding interactions; human ACE2; isothermal titration alorimetry; receptorbinding domain; SARS-CoV-1; SARS-CoV-2description
There are many scientific reports on the interaction of the SARS-CoV-2 virus S protein (and its RBD) with the human ACE2 receptor protein. However, there are no reliable data on how this interaction differs from the interaction of the receptor binding domain of SARS-CoV-1 with ACE2, in terms of binding strength and changes in reaction enthalpy and entropy. Our studies have revealed these differences and the impact of zinc ions on this interaction. Intriguingly, the binding affinity of both RBDs (of SARS-CoV-1 and of SARS-CoV-2) to the ACE2 receptor protein is almost identical; however, there are some differences in the entropic and enthalpic contributions to these interactions.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2023-01-01 | FEBS Open Bio |