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Biophys J, July 2000, p. 357-369, Vol. 79, No. 1

Analysis of Lung Surfactant Model Systems with Time-of-Flight Secondary Ion Mass Spectrometry

Nikolaus Bourdos,* Felix Kollmer,dagger Alfred Benninghoven,dagger Michaela Ross,* Manfred Sieber,* and Hans-Joachim Galla*

 *Institut für Biochemie and  dagger Physikalisches Institut, Westfälische Wilhelms-Universität, D-48149 Münster, Germany

An often-used model lung surfactant containing dipalmitoylphosphatidylcholine (DPPC), dipalmitoylphosphatidylglycerol (DPPG), and the surfactant protein C (SP-C) was analyzed as Langmuir-Blodgett film by spatially resolved time-of-flight secondary ion mass spectrometry (TOF-SIMS) to directly visualize the formation and composition of domains. Binary lipid and lipid/SP-C systems were probed for comparison. TOF-SIMS spectra revealed positive secondary ions (SI) characteristic for DPPC and SP-C, but not for DPPG. SI mapping results in images with domain structures in DPPC/DPPG and DPPG/SP-C, but not in DPPC/SP-C films. We are able to distinguish between the fluid and condensed areas probably due to a matrix effect. These findings correspond with other imaging techniques, fluorescence light microscopy (FLM), scanning force microscopy (SFM), and silver decoration. The ternary mixture DPPC/DPPG/SP-C transferred from the collapse region exhibited SP-C-rich domains surrounding pure lipid areas. The results obtained are in full accordance with our earlier SFM picture of layered protrusions that serve as a compressed reservoir for surfactant material during expansion. Our study demonstrates once more that SP-C plays a unique role in the respiration process.

Biophys J, July 2000, p. 357-369, Vol. 79, No. 1
© 2000 by the Biophysical Society   0006-3495/00/07/357/13  $2.00


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