Interaction of a model apolipoprotein, apoLp-III, with an oil-phospholipid interface

Lipid droplets are “small” organelles that play an important role in de novo synthesis of new membrane, and steroid hormones, as well as in energy storage. The way proteins interact specifically with the oil-(phospho-)lipid monolayer interface of lipid droplets is a relatively unexplored but crucial question. Here, we use our home built liquid droplet tensiometer to mimic intracellular lipid droplets and study protein-lipid interactions at this interface. As model neutral lipid binding protein, we use apoLp-III, an amphipathic α-helix bundle protein. This domain is also found in proteins from the perilipin family and in apoE. Protein binding to the monolayer is studied by the decrease in the oil/water surface tension. Previous work used POPC (one of the major lipids found on lipid droplets) to form the phospholipid monolayer on the triolein surface. Here we expand this work by incorporating other lipids with different physico-chemical properties to study the effect of charge and lipid head-group size. This study sheds light on the affinity of this important protein domain to interact with lipids. [Display omitted] •ApoLp-III has a stronger interaction with an oil-aqueous than an air-aqueous interface.•Phosphatidylcholine prevents interaction of apoLp-III with the oil interface in pure water but not in buffer.•Phosphatidylethanolamine facilitates the interaction of apoLp-III with the lipid-coated oil surface.•Diacylglycerol shows anomalous adsorption behavior at the oil-buffer interface.•Electrostatics controls adsorption of liposomes, and facilitates the interaction of apoLp-III with the oil interface.