The global increase of bacterial resistance to antibiotics has led to increasing interest in research focusing on the development and characterization of new antimicrobial agents. One class of promising antimicrobials found in nature are Antimicrobial Peptides (AMP’s). In contrast to most existing biocides, it is thought that AMPs would share broadly similar modes of membrane disruption. We have designed a novel class of AMPs with the general sequence G(IIKK)nI-NH2, with n = 3-4, denoted as G3 and G4. We propose to compare the binding of these peptides to the spread LPS monolayer with the performance from model biocides SDS, DTAB and trichosan, to identify any structural differences in their membrane attacking processes.