These peptides are highly cationic, made up of similar amino acids, but different in the N- and C-terminal ends. The hydrophobic N-terminal is characterised by six repeats of four amino acids, which are in a conserved sequence: position 1 is always lysine; position 2 is variable; position 3 is always a hydrophobic amino acid or glycine, and in position 4 is either alanine or valine.[1] All members have high antibacterial activity against Gram-positive as well as Gram-negative bacteria at a range of 0.16 to 5 mM concentration. They also exhibit a cytolytic activity between 14.5–24.4 mM on human erythrocytes.