Abstract
Starting from the sequences of magainin 2 analogs, peptides with slightly increased hydrophobic moment ( μ) but retained other structural parameters were designed. Circular dichroism investigations revealed that all peptides adopt an α-helical conformation when bound to phospholipid vesicles. Analogs with increased μ were considerably more active in permeabilizing vesicles mainly composed of zwitterionic lipid. In addition, the antibacterial and hemolytic activities of these analogs were enhanced. Correlation of permeabilization and binding indicated that the activity increase is predominantly caused by an increased membrane affinity of the peptides due to strengthened hydrophobic interactions.
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