Abstract

The airspaces are lined with a DPPC-rich film called pulmonary surfactant, named for its ability to maintain normal respiratory mechanics by reducing surface tension at the air/liquid interface. Inhaled airborne particles containing smooth bacterial lipopolysaccharide (s-LPS) might incorporate into the surfactant monolayer. In this study, we evaluated the effect of s-LPS on the behavior of DPPC films by using epifluorescence microscopy combined with a surface balance. In addition, we investigated whether LPS effects could be counteracted by surfactant protein A (SP-A), which is a LPS binding protein, with the peculiarity that this protein is associated to the surfactant monolayer. Thus SP-A is in the initial defence barrier against inhaled airborne particles. Our data show that s-LPS injected in the aqueous subphase penetrated into DPPC films to form mixed DPPC/s-LPS monolayers. Low amounts of s-LPS fluidized the DPPC monolayer, as demonstrated by fluorescence microscopy and changes in the compressibility modulus. This promoted early collapse and prevented the attainment of high surface pressures. The interaction of SP-A with DPPC/s-LPS film further fluidized the monolayers and facilitated the extraction of s-LPS at surface pressures where SP-A was expelled from the mixed films, suggesting that SP-A is an LPS scavenger. A better understanding of the biophysical properties of lung surfactant monolayer and its susceptibility to LPS inhibition is important for the development of new surfactant formulations for respiratory diseases.

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