Dermaseptin proteins are used in eukaryotes as an antimicrobial agent. Dermaseptins are typically between 30 to 76 amino acids in length. This domain is found associated with PF03032. The full-length protein is almost completely defined in an alpha helical domain. It creates high levels of disorder at the level of the phospholipid head group of bacterial membranes suggesting that it partitions into the bilayer where it severely disrupts membrane packing. The polypeptide precursor to the dermaseptins consist of a tripartite organisation: a N-terminal signal peptide, followed by an acidic region terminated by two basic Lys-Arg residues and the actual dermaseptin at the C terminus.