New insight into the mechanism of action of the temporin antimicrobial peptides

Two members, temporin A (TA) and temporin L (TL) from temporins which constitute a family of amphipathic [alpha]-helical antimicrobial peptides (AMPs) and contain some of the shortest cytotoxic peptides are examined to understand their spectra of antimicrobial activity and toxicity. NMR studies indicated that strongly hemolytic [Gln.sup.3]-TA exhibited stable helical conformation along the entire sequence, while weakly hemolytic but antimicrobial [Pro.sup.3]-TL showed conformational averaging at the N-terminus.