Interaction forces between DPPC bilayers on glass.

The surface force apparatus (SFA) was utilized to obtain force-distance profiles between silica-supported membranes formed by Langmuir-Blodgett deposition of 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC). In the absence of a membrane, a long-range electrostatic repulsion and short-range steric repulsion are measured as a result of the deprotonation of silica in water and the roughness of the silica film. The electrostatic repulsion is partially screened by the lipid membrane, and a van der Waals adhesion comparable to that measured with well-packed DPPC membranes on mica is measured. This finding suggest that electrostatic interactions due to the underlying negatively charged silica are likely present in other systems of glass-supported membranes. In contrast, the charge of an underlying mica substrate is almost completely screened when a lipid membrane is deposited on the mica. The difference in the two systems is attributed to the stronger physisorption of zwitterionic lipids to molecularly smooth mica compared to physisorption to rougher silica.

Impact of membrane fluidity on steric stabilization by lipopolymers.

In this work, the impact of lipid lateral mobility on the steric interaction between membranes containing poly(ethylene glycol) (PEG) functionalized lipids was investigated using the surface force apparatus. The force-distance profiles show the presence of electrostatic and steric repulsion that arise from the presence of negatively charged PEG functionalized lipids. Fluid-phase bilayers have high lateral diffusion relative to gel-phase bilayers; however, a quantitative comparison of the interaction forces between membranes in these two different phase states demonstrates a reduced rate of diffusion in the fluid phase for the PEG-lipids under constrained geometries. Thus, the amount of polymer in the contact zone can be modulated and is reduced with fluid membranes; however, complete exclusion was not achieved. As a result, the steric repulsion afforded by PEG chains or binding affinity of ligated PEG chains can only be modestly tailored by the phase state of the liposome.