Direct observation of phase and morphology changes induced by lung surfactant protein SP-B in lipid monolayers via fluorescence, polarized fluorescence, Brewster angle, and atomic force microscopies

Ka Yee C. Lee; Michael M. Lipp; Joseph A. N. Zasadzinski; Alan J. Waring

doi:10.1117/12.306121

24 April 1998 Direct observation of phase and morphology changes induced by lung surfactant protein SP-B in lipid monolayers via fluorescence, polarized fluorescence, Brewster angle, and atomic force microscopies

Ka Yee C. Lee, Michael M. Lipp, Joseph A. N. Zasadzinski, Alan J. Waring

Author Affiliations +

Proceedings Volume 3273, Laser Techniques for Condensed-Phase and Biological Systems; (1998) https://doi.org/10.1117/12.306121
Event: Optoelectronics and High-Power Lasers and Applications, 1998, San Jose, CA, United States

Abstract

Both human lung surfactant protein SP-B and its amino terminus alter the phase behavior of palmitic acid (PA) monolayers by inhibiting the formation of condensed phases and creating a new fluid PA-protein phase. This phase increase the compressibility of the monolayers by forming a network that separates condensed phase domains at coexistence and persists to high surface pressures. The network changes the monolayer collapse nucleation from a heterogenous to a more homogenous process through isolating individual condensed phase domains. This results in higher surface pressures at collapse, and monolayers easier to respread on expansion, factors essential to the in vivo function of lung surfactant. The network is stabilized by low line tension between the coexisting phases are confirmed by the formation of extended linear domains or 'stripe' phases. Similar stripes are found in monolayers of fluorescein-labeled amino terminus, suggesting that the reduction n line tension is due to the protein. Comparison of isotherm data and observed morphologies of monolayers containing amino terminus with those containing amino terminus with those containing the full length SP-B protein shows that the peptide retains most of the native activity of the protein, which may lead to cheaper and more effective synthetic replacement formulations.

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Ka Yee C. Lee, Michael M. Lipp, Joseph A. N. Zasadzinski, and Alan J. Waring "Direct observation of phase and morphology changes induced by lung surfactant protein SP-B in lipid monolayers via fluorescence, polarized fluorescence, Brewster angle, and atomic force microscopies", Proc. SPIE 3273, Laser Techniques for Condensed-Phase and Biological Systems, (24 April 1998); https://doi.org/10.1117/12.306121

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