GALA is a synthetic pH sensitive peptide designed to better understand viral fusion proteins interaction with membranes. This could ultimately lead to better drug delivery systems by more efficient cell entry and escape from the endosome to enter the nucleus.

GALA is 30 amino acids long, sufficient to span the lipid bilayer. The EALA repeats are designed to create a hydrophobic face that can allow lipid interaction when GALA is in an alpha helical conformation. Glutamic acid is inserted with the EALA repeats to create a pH-dependent negatively charged sidechain.  In neutral pH conditions GALA is in a random coil conformation. In acidic conditions (pH 5) GALA forms an amphipathic helix which can bind to the lipid bilayer. The interaction varies depending on the composition of the lipid membrane. Most importantly, interaction with negative or neutrally-charge bilayers leads to the formation of a transbilayer pore formed of approximately 10 GALA peptides. GALA has already been utilised for this purpose at low pH to deliver genes into the nucleus of cells in vitro. The composition of the membrane effects the formation and bilayer-destabilizing properties of GALA however, GALA has a strong potential for future applications for the delivery of genes, DNA and drugs into the cell.