Interaction of adrenocorticotropin-(1-24)-tetracosapeptide with lipid bilayers.

The interaction of the peptide hormone adrenocorticotropin with solvent-free planar lipid bilayers (BLM) and liposomes was studied by measurements of elasticity modulus perpendicular to the plane of the membrane (E perpendicular, measured by electrostriction), surface potential difference (delta phi m), electrical capacitance, capacitance relaxation following a voltage jump (yielding relaxation times for molecular dipoles or dipolar domains), and fluorescence polarization. Addition of the 6-fold positively charged peptide to one side of the membrane leads to a more positive membrane surface potential, an increase of BLM capacitance, a decrease of elasticity modulus, and faster relaxation time constants. This also caused a decrease of DPH fluorescence anisotropy of the liposome suspension modified by fluorescent dye DPH. Mixed BLM of palmitoyl-oleoyl-phosphatidylcholine (POPC)+soybean phosphatidylcholine (SBPC) (10:1 w/w), which carry a negative surface charge, exhibit considerably larger changes than electroneutral POPC membranes. Our results confirm that ACTH1-24 binds to BLM and interacts with the hydrophobic part of the bilayer.