Surfactant protein interactions with neutral and acidic phospholipid films

Abstract

The captive bubble tensiometer was employed to study interactions of phospholipid (PL) mixtures of dipalmitoylphosphatidylcholine (DPPC) and 1-palmitoyl-2-oleoyl- sn-glycero-3-phosphocholine (POPC) or 1-palmitoyl-2-oleoyl- sn-glycero-3-[phospho- rac-(1-glycerol)] (POPG) at 50 μg/ml with physiological levels of the surfactant protein (SP) A SP-B, and SP-C alone and in combination at 37°C. All surfactant proteins enhanced lipid adsorption to equilibrium surface tension (γ), with SP-C being most effective. Kinetics were consistent with the presence of two adsorption phases. Under the conditions employed, SP-A did not affect the rate of film formation in the presence of SP-B or SP-C. Little difference in γmin was observed between the acidic POPG and the neutral POPC systems with SP-B or SP-C with and without SP-A. However, γmax was lower with the acidic POPG system during dynamic, but not during quasi-static, cycling. Considerably lower compression ratios were required to generate low γminvalues with SP-B than SP-C. DPPC-POPG-SP-B was superior to the neutral POPC-SP-B system. Although SP-A had little effect on film formation with SP-B, surface activity during compression was enhanced with both PL systems. In the presence of SP-C, lower compression ratios were required with the acidic system, and with this mixture, SP-A addition adversely affected surface activity. The results suggest specific interactions between SP-B and phosphatidylglycerol, and between SP-B and SP-A. These observations are consistent with the presence of a surface-associated surfactant reservoir which is involved in generating low γ during film compression and lipid respreading during film expansion.