reflects the impact of this AA change on the stability of the helical peptide structures. Additionally, quantum methods confirm this observation and remark on the importance of Asn on peptide reactivity . Although the predicted tridimensional structures of the peptides forming activity cliffs are similar (pairs 3 (AP03010 -AP02656); 4 (AP03010 -AP03022); and 5 (AP03010 -AP03311 in Figures and), their values of volume of accessible surface area are different which suggest changes in their solubility (Table in the Supplementary material). Such differences could be associated with changes in their biological activity . Additionally, the differences between the cationic area (involved in the membrane interaction on MRSA strains) of each peptide pair could be associated with their variations in biological activity (Table in the Supplementary material).