ACE2 fragment as a decoy for novel SARS-Cov-2 virus

Fabiana Renzi; Dario Ghersi

We identified a minimal ACE2 fragment consisting of two α-helices that retains most of the key interactions with the S protein without interfering with its physiological ligand an-giotensinII. Using molecular dynamics (MD) simulations we confirmed that the peptide remains stable in complex with the S-protein. Further, the peptide appears to be stable in an aqueous environment. We conclude by highlighting the potential therapeutic applications of this peptide in terms of scalability, lack of toxicity and immunogenicity, possible administration routes, and potential applications in diagnostic tests. dinates of the S-protein in the pre-fusion conformation (conformation 3 with CTD1 open at 111.6º, which is the physiological state when the S protein binds to the ACE2 receptor). The comparison of the crystal and EM structures did not show evident deviations in the tertiary or secondary structure in regions corresponding to the S-protein binding site (not shown).