Eukaryotic organisms rely on several mechanisms to inhibit bacterial growth and infection, which mankind has sought to mimic to their specific and more targeted use. Due to the effect of adaptation by bacteria in response to new antibiotics, known as antibiotic resistance, there will be an ever-present need to develop new antibiotics to maintain their high efficiency. Peptide antibiotics appear to target a general property of the bacterial membrane, and should therefore constitute a mechanism which is highly robust to mutational adaptation. We employ a specialized implementation of molecular dynamics simulations to examine the membrane-interactions and -permeabilization caused by human dermcidin in bacterial membranes, which shows antibacterial properties in experiment and forms a transmembrane channel-like structure according to a solved crystal structure. We are able to conclude that charged sidechains maintain a structural rigidity of the oligomeric assembly which in turn enables it to maintain anion selectivity, and that lower oligomeric states constitute an potentially functional oligomeric precursor to the crystallized hexamer. Further we are able to improve channel conductance, and suggest experimental observables to corroborate the given conclusions. The knowledge gained forwards the knowledge-base needed to establish a categorization of the class of AntiMicrobial Peptides, and holds promise for further development as a possible broad-spectrum antibiotic.