Peptides derived from α-lactalbumin membrane binding helices oligomerize in presence of lipids and disrupt bilayers

From left to right: alpha-lactalbumin has two membrane active helices, Helix A and Helix C. Two chimeric peptides were prepared to see if taking these peptides out of the protein fold would enhance their ability to interact with the membrane. Tryptophan fluorescence showed that the segments of each peptide were intercalated in the membrane to varying degrees. They also disrupted vesicles in a pH-dependent manner and formed oligomers on solid supported bilayers.138