Kinetics of the adhesion of DMPC liposomes on a mercury electrode. Effect of lamellarity, phase composition, size and curvature of liposomes, and presence of the pore forming peptide mastoparan X.
Liposomes suspended in aqueous electrolyte solutions can adhere at mercury electrodes. The adhesion is a complex process that starts with the docking and opening and leads to a spreading, finally resulting in the formation of islands of adsorbed lecithin molecules. The adhesion process can be followed by chronoamperometry, and a detailed analysis of the macroscopic and microscopic kinetics can be performed yielding rate constants and activation parameters. By using giant unilamellar liposomes and multilamellar liposomes, the effect of lamellarity and liposome size could be elucidated for liposomes in the liquid crystalline, gel, and superlattice phase states. Below the phase transition temperature, the time constant of opening of the liposomes (i.e., the irreversible binding of the lecithin molecules on the preliminary contact interface liposome|mercury and the therewith associated disintegration of the liposome membrane on that spot) is shown to be strongly size dependent. The activation energy, however, of that process is size independent with the exception of very small liposomes. That size dependence of time constants is a result of the size dependence of the initial contact area. The time constant and the activation energies of the spreading step exhibit a strong size dependence, which could be shown to be due to the size dependence of rate and activation energy of pore formation. Pore formation is necessary to release the solution included in the liposomes. This understanding was corroborated by addition of the pore inducing peptide Mastoparan X to the liposome suspension. The obtained results show that electrochemical studies of liposome adhesion on mercury electrodes can be used as a biomimetic tool to understand the effect of membrane properties on vesicle fusion.
Hernandez
Victor Agmo
VA
Institut für Biochemie, Universität Greifswald, 17489 Greifswald, Soldmannstr. 23, Germany.
Scholz
Fritz
F
D000327:Adsorption; D004134:Dimyristoylphosphatidylcholine / Q000737:chemistry*; D004566:Electrodes; D036341:Intercellular Signaling Peptides and Proteins; D007700:Kinetics; D008081:Liposomes / Q000737:chemistry*; D008628:Mercury / Q000737:chemistry*; D010316:Particle Size; D010455:Peptides / Q000737:chemistry*; D013499:Surface Properties
D036341:Intercellular Signaling Peptides and Proteins; D008081:Liposomes; D010455:Peptides; C071123:mastoparan X; D008628:Mercury; D004134:Dimyristoylphosphatidylcholine