Biopolymers and cell. 1999; 15 (6): 481 - 486

Lysozyme interaction with liposomes: thermodynamics of binding

G. P. Gorbenko

Using the method of competitive analysis the interaction of lysozyme with liposomes composed of phosphatidyicholine and diphosphatidylglycerot has been studied. In terms of the lattice and continuum models of large ligand adsorption to membrane thermodynamic parameters for the protein-lipid complexes have been estimated. Lysozyme binding to liposomes containing more than 25 mot % of DPG has been found to be characterized by the positive cooperativity, originating, presumably, from the self-association of the bound protein.