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It is known that bacterial lipoproteins confer sensitivity to the bactericidal activity of cationic peptides. In this study, we found that the mechanism of interaction between SaBPs and *S. aureus* is mediated by the lipoteichoic acid layer of the cell wall, which plays an important role in binding and entrance into the bacterial cell \[[@bib40]\]. The relatively high concentration of calcium in the composition of SaBPs increases the solubility of these peptides and facilitates their access to the membrane, which is modified by the hydrophobic portion of lipoteichoic acid. The mechanism of interaction is likely the result of an electrostatic force between the positive charges of the peptide and the negative charge of the lipoteichoic acid. As no other peptides have showed activity against MRSA, the broad-spectrum activity of SaBPs against a range of *S. aureus* clinical isolates can be attributed to the lipophilic content and positive charge of these peptides \[[@bib41]\]. The strong electrostatic interaction of the Ca^2+^ ion present in the BPs with staphylococcal lipoteichoic acid results in a major enhancement of their affinity for *S. aureus* and other bacteria, as was also observed for *E. coli* \
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