Adsorption, compression and stability of surface films from natural, lipid extract and reconstituted pulmonary surfactants

Abstract

A pulsating bubble surfactometer was used to study the surface activities and surface film stabilities of bovine pulmonary surfactants (10 mg/ml) and a reconstituted surfactant (10 mg/ml). Pulmonary surfactants were natural surfactant (NS), lipid extract surfactant [LES(chol)] and lipid extract surfactant without neutral lipids (LES). NS is composed of phospholipids, neutral lipids and surfactant-associated proteins (SP-A, SP-B and SP-C). Both LES(chol) and LES are organic solvent extracts of NS. LES(chol) retains all the components of NS except SP-A. Reconstituted surfactant was dipalmitoylphosphatidylcholine (DPPC): 1-palmitoyl-2-oleoyl-phosphatidylglycerol (POPG): SP-B/7:3:1%. All three pulmonary surfactants attained the equilibrium surface tension almost instantaneously at 37 degrees C. The adsorption rates of NS and LES(chol) at 24 degrees C were similar to those at 37 degrees C, while LES exhibited a lower adsorption rate at 24 degrees C. Reconstituted surfactant adsorbed slower than any of the pulmonary surfactants. Film stability was studied by recording the spontaneous increase in the pressure gradient of a static bubble at the minimum size (Rmin) once near zero surface tension was attained. The order of surface film stabilities were: reconstituted surfactant > > NS > LES > LES(chol). Surface films of NS and LES could be stabilized by prolonged pulsation, while film stability of LES(chol) was only moderately affected by pulsation. These results indicate that SP-A in NS promotes formation of some unique structure, possibly tubular myelin, which induces selective adsorption of lipids into the surface.