期刊
LANGMUIR
卷 28, 期 20, 页码 7811-7825出版社
AMER CHEMICAL SOC
DOI: 10.1021/la301134v
关键词
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资金
- Spanish Direccion General de Investigacion [BIO2009-09694, BFU2009-08401, BFU2010-11538, CSD2007-00010]
- Community of Madrid [S2009MAT-1507]
- Generalitat Valenciana
- University of Nuevo Leon
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 facilitating compression-driven condensation of domains in anionic phospholipid films as observed by epifluorescence microscopy. Finally, both native palmitoylated SP-C and the phenylalanine-containing recombinant versions facilitate similarly the repetitive compression expansion dynamics of lipid/protein films, which were able to reach maximal surface pressures with practically no hysteresis along multiple quasi-static or dynamic cycles.
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