Abstract
Phospholipids are ubiquitous components of biomembranes and common biomaterials used in many bioengineering applications. Understanding adsorption of phospholipids at the air-water surface plays an important role in the study of pulmonary surfactants and cell membranes. To date, however, the biophysical mechanisms of phospholipid adsorption are still unknown. It is challenging to reveal the molecular structure of adsorbed phospholipid films. Using combined experiments with constrained drop surfactometry and molecular dynamics simulations, here, we studied the biophysical mechanisms of dipalmitoylphosphatidylcholine (DPPC) adsorption at the air-water surface. It was found that the DPPC film adsorbed from vesicles showed distinct equilibrium surface tensions from the DPPC monolayer spread via organic solvents. Our simulations revealed that only the outer leaflet of the DPPC vesicle is capable of unzipping and spreading at the air-water surface, whereas the inner leaflet remains intact and forms an inverted micelle to the interfacial monolayer. This inverted micelle increases the local curvature of the monolayer, thus leading to a loosely packed monolayer at the air-water surface and hence a higher equilibrium surface tension. These findings provide novel insights, to our knowledge, into the mechanism of the phospholipid and pulmonary surfactant adsorption and may help understand the structure-function correlation in biomembranes.