The interactionofmany lytic cationic antimicrobial peptides with their target cells involves electrostatic interactions, hydrophobic effects, and the formation of amphipathic sec-ondary structures, such asahelices orbsheets. We have shown in previous studies that incorporating 30% D-aminoacids intoashortahelical lyticpeptidecomposedof leucine and lysine preserved the antimicrobial activity of the parent peptide, while the hemolytic activity was abolished.