Abstract:
The lead optimization of an antimicrobial hexapeptide Orn-D-Trp-D-Phe-Ile-D-Phe-His(1-Bzl)-NH2 depending on the hydrophobic or positive-charge character of amino acids at various positions along its sequence was performed, followed by biological evaluation and mechanistic studies. This led to the identification of a new class of antimicrobial hexapeptides that interact preferentially with the negatively charged phospholipids of a model bacterial membrane.