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Structure of SP-B/DPPC mixed films studied by neutron reflectometry.

Fullagar, W K; Holt, S A; Gentle, I R.
Biophys J; 95(10): 4829-36, 2008 Nov 15.
Artigo em Inglês | MEDLINE | ID: mdl-18708453
The structures of films of pulmonary surfactant protein B (SP-B) and mixtures of SP-B and dipalmitoylphosphatidylcholine (DPPC) at the air/water interface have been studied by neutron reflectometry and Langmuir film balance methods. From the film balance studies, we observe that the isotherms of pure DPPC and SP-B/DPPC mixtures very nearly overlay one another at very high pressures, suggesting that the SP-B is being excluded from the film. The use of multiple contrasts with neutron reflectometry at a range of surface pressures has enabled the mixing and squeeze out of the DPPC and SP-B mixtures to be studied. We can identify the SP-B component of the interfacial structure and its position as a function of surface pressure. The mixtures are initially a homogeneous layer at low surface pressures. At higher surface pressures, the SP-B is squeezed out of the lipid layer into the subphase, with the first signs detected at 30 mN m(-1). At 50 mN m(-1), the subphase is almost completely excluded from the DPPC layer, with the SP-B content significantly reduced. Only a small amount of DPPC appears to be associated with the squeezed out SP-B.
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