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Has the human biological interaction with SARS-CoV2 variants entered a pliant “Faustian bargain”?

by | Jul 9, 2024 | Scientific reports, Virology, Pathophysiology

By Richard J. Head et al.

Source British Pharmacological Society

We have highlighted recently1 the importance of the affinity of SARS-CoV2 for its target the Angtiontensin II (ACEII) receptor, and in fundamental thermodynamic terms, this affinity is linked to the passage of the virus from the airway and its subsequent diffusion across the mucosa. This relationship of infectivity and pathophysiology in the upper airway is key to understanding the morbidity and mortality of this pandemic. For example, the dissociation constant, Kd, of SARS-CoV is 5.0 nM, while that of SARS-CoV-2 is 1.2 nM, at 30°C.2 These values can be used to find Gibbs energy of binding, which is: ΔBG0 = −48.2 kJ/mol for SARS-CoV and ΔBG0 = −51.8 kJ/mol for SARS-CoV-2. Thus, SARS-CoV-2 has a 1.075 × greater binding affinity than SARS-CoV.

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