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The behavior at air–liquid interfaces of two recombinant versions of human surfactant protein SP-C has been characterized in comparison with that of native palmitoylated SP-C purified from porcine lungs. Both native and recombinant proteins promoted interfacial adsorption of dipalmitoylphosphatidylcholine bilayers to a limited extent, but catalyzed very rapid formation of films from different lipid mixtures containing both zwitterionic and anionic phospholipids. Once at the interface, the recombinant variants exhibited compression-driven structural transitions, consistent with changes in the orientation of the deacylated N-terminal segment, which were not observed in the native protein. Compression isotherms of lipid/protein films suggest that the recombinant SP-C forms promote expulsion at high pressures of a higher number of lipid molecules per mole of protein than does native SP-C. A more dynamic conformation of the N-terminal segment in recombinant SP-C forms is likely also responsible for facilitatin...
| Authors: | Dunja Lukovic; Antonio Cruz; Azucena Gonzalez-Horta; Andrea Almlen; Tore Curstedt; Ismael Mingarro; Jesus Pérez-Gil | |
| Journal: | Langmuir | |
| Year: | 2012 | |
| DOI: | 10.1021/la301134v | |
| Publication date: | 10-05-2012 |
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