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The apoptosis inducing (pro-apoptotic) peptide sequence, D-(KLAKLAK)2, has been classified as a potent antimicrobial agent [1]. Moreover, it was found to trigger cell death in bacteria without inducing cytotoxicity in mammalian cell types. The chemical basis for this selectivity has been associated with the poly(cationic) amphiphilic nature of this peptide sequence, which facilitates cell permeability in negatively charged bacterial membranes and not within the zwitterionic lipid bilayers of mammalian cell types [1,2]. Upon cell internalization, the positively charged D-(KLAKLAK)2 sequence accumulates on the surface of the mitochondria and induces depolarization of the negatively charged mitochondrial membrane [3]. This depolarization compromises the mitochondrial membrane integrity and triggers the release of cell death effectors, including cytochrome c, second mitochondrial derived activator of caspase and the apoptosis-inducing factor (AIF) which ultimately results in the programmed cell death response [4]. Considering the potential of this antimicrobial peptide sequence in the treatment of infectious diseases, an optimized solid-phase peptide synthesis and structure analyses by Circular Dichroism (CD) spectroscopy is revealed in this study.

Solid-Phase Peptide Synthesis and Structural Analyses by Circular Dichroism Spectroscopy of the Cytotoxic D-(KLAKLAK)2 Sequence