Pressure-induced changes in the molecular organization of a lipid-peptide complex: polymyxin binding to phosphatidic acid membranes.
The effect of 100 atm pressure on the organization of the lipid-peptide complex formed between polymyxin and dipalmitoyl phosphatidic acid has been investigated. Phase transition curves were obtained by electron paramagnetic resonance by measuring the partition coefficient of the spin label, 2, 2, 5, 5-tetramethylpiperidine-N-oxyl. The three-step phase transition curve previously obtained with fluorescence polarization measurements was confirmed, demonstrating three distinct phosphatidic acid domains in the bilayer. Pressure increases binding of polymyxin to phosphatidic acid bilayers and alters the proportions of the two domains that differ in the mode of binding between phosphatidic acid and polymyxin. The binding curves of polymyxin to phosphatidic acid bilayers wre determined and it was shown that application of pressure reduces the cooperativity of the binding curve.
D001665:Binding Sites; D008055:Lipids; D008081:Liposomes; D008968:Molecular Conformation; D010455:Peptides; D010712:Phosphatidic Acids; D011112:Polymyxin B; D011113:Polymyxins; D011312:Pressure; D013816:Thermodynamics
D008055:Lipids; D008081:Liposomes; D010455:Peptides; D010712:Phosphatidic Acids; D011113:Polymyxins; D011112:Polymyxin B