Conclusion: As could be anticipated, most of the studied mutations act as protein-protein interface destabilizers; however, a non-negligible number of mis-sense variations are predicted to enhance ACE2/
S-RBDCoV-2 binding; in particular, the variants Q24T, T27D/K/W, D30E, H34S/T/K, E35D, Q42K,
L79I/W, R357K, and R393K on ACE2 and
L455D/W, F456 K/W,
Q493K,
N501T, and
Y505W on the
S-protein
receptor binding domain, respectively, are expected to increase the affinity of each mutant isoforms for the corresponding protein counterpart.