We also study the sequence alignment of the twenty most active peptides within our dataset shows a consensus sequence ("GCRANKGACRAKKCKSHGGRGGKCF" -Figure in the Supplementary material), having a high net charge of +8.25 and 32% hydrophobic ratio. We remark on the presence of four cysteines (Cys -C) in the peptide sequence, which contributes to the stability of the tertiary structure . The presence of four cysteines is also observed in anti-MRSA peptidic sequences, for example in peptides AP03010, AP03022, and AP03311 in Figure (vide infra).