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The antimicrobial peptide KLKKLK-NH 2  was developed based on sapesin B, and synthesized using D-amino acids. Biochemical properties of the D-form and L-form KLKKLK-NH 2  peptides were compared. In order to limit the effects due to bacterial resistance to proteolysis, antimicrobial activities of the peptides were evaluated after short-term exposure to bacteria. D-form KLKKLK-NH 2  exhibited higher antimicrobial activities than L-form KLKKLK-NH 2  against bacteria, including  Staphylococcus aureus  and  Escherichia coli . In contrast, both the D-form and L-form of other antimicrobial peptides, including Mastoparan M and Temporin A, exhibited similar antimicrobial activities. Both the D-form KLKKLK-NH 2  and L-form KLKKLK-NH 2  peptides preferentially disrupted  S. aureus -mimetic liposomes over mammalian-mimetic liposomes. Furthermore, the D-form KLKKLK-NH 2  increased the membrane permeability of  S. aureus  more than the L-form KLKKLK-NH 2 . Thus suggesting that the enhanced antimicrobial activity of the D-form was likely due to its interaction with bacterial cell wall components.  S. aureus  peptidoglycan preferentially inhibited the antimicrobial activity of the D-form KLKKLK-NH 2  relative to the L-form. Furthermore, the D-form KLKKLK-NH 2  showed higher affinity for  S. aureus  peptidoglycan than the L-form. Taken together, these results indicate that the D-form KLKKLK-NH 2  peptide has higher antimicrobial activity than the L-form via a specific association with bacterial cell wall components, including peptidoglycan.

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D-form KLKLLLLLKLK-NH2 peptide exerts higher antimicrobial properties than its L-form counterpart via an association with bacterial cell wall components