The detrimental effect of serum albumin on the re-spreading of a dipalmitoyl phosphatidylcholine Langmuir monolayer is counteracted by a fluorocarbon gas
Biochimica et Biophysica Acta (BBA) - Biomembranes, ISSN: 0005-2736, Vol: 1768, Issue: 3, Page: 490-494
2007
- 17Citations
- 17Captures
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Article Description
We have recently reported that fluorocarbon gases exhibit an effective fluidizing effect on Langmuir monolayers of dipalmitoyl phosphatidylcholine (DPPC), preventing them from crystallizing up to surface pressures of ∼ 40 mN m −1, i.e. well above the DPPC's equilibrium surface pressure. We now report that gaseous perfluorooctyl bromide (gPFOB) promotes the re-spreading of DPPC Langmuir monolayers compressed on a bovine serum albumin (BSA)-containing sub-phase. The latter protein is known to maintain a concentration-dependent surface pressure that can exceed the re-spreading pressure of collapsed monolayers. This phenomenon was proposed to be responsible for lung surfactant inactivation. Compression/expansion isotherms and fluorescence microscopy experiments were carried out to assess the monolayers' physical state. We have found that, during expansion under gPFOB-containing air, the surface pressure of a DPPC monolayer on a BSA-containing sub-phase decreased to much lower values than when the DPPC monolayer was expanded in the presence of BSA under air (∼ 0 mN m −1 vs. ∼ 7.5 mN m −1 at 120 Å 2, respectively). Moreover, fluorescence images showed that, during expansion, the BSA-coupled DPPC monolayers, in contact with gPFOB, remained in the liquid-expanded state for surface pressures lower than 10 mN m −1, whereas they were in a liquid-condensed semi-crystalline state, even at large molecular areas (120 Å 2 ), when expanded under air. The re-incorporation of the PFOB molecules in the DPPC monolayer during expansion thus competes with the re-incorporation of BSA, thus preventing the latter from penetrating into the DPPC monolayer. We suggest that combinations of DPPC and a fluorocarbon gas may be useful in the treatment of lung conditions resulting from a deterioration of the native lung surfactant function due to plasma proteins, such as in the acute respiratory distress syndrome.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0005273606003816; http://dx.doi.org/10.1016/j.bbamem.2006.09.022; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=33847035574&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/17097604; https://linkinghub.elsevier.com/retrieve/pii/S0005273606003816; https://dx.doi.org/10.1016/j.bbamem.2006.09.022
Elsevier BV
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