Login / Signup

Thermodynamic analysis of the interactions between human ACE2 and Spike RBD of Betacoronaviruses (SARS-CoV-1 and SARS-CoV-2).

Agnieszka Rombel-BryzekAdriana MillerDanuta Witkowska
Published in: FEBS open bio (2022)
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 as well as 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.
Keyphrases
  • sars cov
  • respiratory syndrome coronavirus
  • binding protein
  • endothelial cells
  • angiotensin converting enzyme
  • angiotensin ii
  • protein protein
  • mass spectrometry
  • pluripotent stem cells
  • transcription factor