Tryptophan substitutions reveal cooperative membrane transitions and aromatic interactions associated with membrane permeabilisation in CM15 and MSI-78 peptide analogues.
Antimicrobial peptides CM15 (Ac-KWKLFKKIGAVLKVL-NH2) and MSI-78(11-22)-NH₂ (Ac-CKFGKAFVKILKK-NH2) have remarkable abilities to interact with negatively charged lipid bilayers, adopting helical secondary structures while embedded within the membrane, and, with increasing peptide concentration, evolving toward aggregatio...