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The hydrophobicity (H), hydrophobic moment (μ) and the angle subtended by the positively charged helix face (Φ) of a set of model and magainin2amide peptides with conserved charge and helix propensity have been shown to be effective modulators of antibacterial and haemolytic activity. Except peptides of low hydrophobicity which are inactive, changing the parameters has little influence on the activity...
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...
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