GALA is a 30 amino acid synthetic peptide with a glutamic acid-alanine-leucine-alanine (EALA) repeat. It also contains a histidine and tryptophan residue as spectroscopic probes. This peptide was designed to explore how viral fusion protein sequences interact with membranes. It was used to study the importance of the helix length, hydrophobicity, and hydrophobic moment on the formation, structure, and function of ion channels. The membrane-interacting properties of GALA have been extensively documented. Investigations with analogs of cytotoxic peptides clarify the importance of peptide charge and the role of particular amino acids or arrays of amino acids in the conformation, membrane-binding affinity, and pore-forming abilities of these toxins.