Fig. 9. BAlaS-guided design of tight-binding peptides. (a) Propensity scale of each amino acid to form an α-helical peptide conformation. (b) Sequences of designed peptides p12–p16. Scatter plots with predicted BAlaS ΔΔG = ΔGAla − ΔGwt values on substitution to alanine for each residue of (c) the 11 Mpro natural substrates and (d) designed peptides based on these. The more positive the value, the greater the contribution made by the sidechain to the overall binding energy. (e) The BAlaS ΔΔGSum comparing values between complexes of Mpro with substrate and designed peptides as a proxy for predicting relative binding affinity (larger score = tighter binder).
