Interaction of soluble and membrane proteins with monolayers of glycosphingolipids.

Abstract

1. The interactions of four proteins (albumin, myelin basic protein, melittin and glycophorin) with eight neutral or acidic glycosphingolipids, including sulphatides and gangliosides, five zwitterionic or anionic phospholipids and some of their mixtures, were studied in lipid monolayers at the air/145 mM-NaCl interface. 2. In lipid-free interfaces, the surface pressure and surface potential reached by either soluble or integral membrane proteins did not reveal marked differences. 3. All the proteins studied showed interactions with each of the lipids but the maximal interactions were found for basic proteins with acidic glycosphingolipids. 4. Surface-potential measurements indicated that different dipolar organizations at the interface can be adopted by lipid-protein interactions showing the same value for surface free energy. 5. The individual surface properties of either the lipid of protein component are modified as a consequence of the lipid-protein interaction. 6. In mixed-lipid monolayers, the composition of the interface may affect the lipid-protein interactions in a non-proportional manner with respect to the relative amount of the individual lipid components.