Influence of tryptophan on lipid binding of linear amphipathic cationic antimicrobial peptides

Research shows that analogues of the amphipathic beta-sheet structure forming peptides, which contain tryptophan, exhibit strikingly different lipid binding and lytic activity between the alpha-helical and beta-sheet peptides than the parent peptides without tryptophan residues. However, both peptide types show similar antimicrobial activity.