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Micropipette Technique Study of Natural and Synthetic Lung Surfactants at the Air-Water Interface: Presence of a SP-B Analog Peptide Promotes Membrane Aggregation, Formation of Tightly Stacked Lamellae, and Growth of Myelin Figures.

Publication ,  Journal Article
Parra, E; Kinoshita, K; Needham, D
Published in: Langmuir : the ACS journal of surfaces and colloids
October 2016

The present study is a microscopic interfacial characterization of a series of lung surfactant materials performed with the micropipette technique. The advantages of this technique include the measurement of equilibrium and dynamic surface tensions while acquiring structural and dynamic information at microscopic air-water interfaces in real time and upon compression. Here, we characterized a series of animal-derived and synthetic lung surfactant formulations, including native surfactant obtained from porcine lungs (NS); the commercial Curosurf, Infasurf, and Survanta; and a synthetic Super Mini-B (SMB)-containing formulation. It was observed that the presence of the natural hydrophobic proteins and, more strikingly, the peptide SMB, promoted vesicle condensation as thick membrane stacks beneath the interface. Only in the presence of SMB, these stacks underwent spontaneous structural transformations, consisting of the nucleation and growth of microtubes and in some cases their subsequent coiling into helices. The dimensions of these tubes (2-15 μm diameter) and their linear (2-3 μm/s) and volumetric growth rates (20-30 μm3/s) were quantified, and no specific effects were found on them for increasing SMB concentrations from 0.1 to 4%. Nevertheless, a direct correlation between the number of tubes and SMB contents was found, suggesting that SMB molecules are the promoters of tube nucleation in these membranes. A detailed analysis of the tube formation process was performed following previous models for the growth of myelin figures, proposing a combined mechanism between dehydration-rehydration of the lipid bilayers and induction of mechanical defects by SMB that would act as nucleation sites for the tubes. The formation of tubes was also observed in Infasurf, and in NS only after subsequent expansion and compression but neither in the other clinical surfactants nor in protein-free preparations. Finally, the connection between this data and the observations from the lung surfactant literature concerning the widely reported "near-zero surface tension" for lung surfactant films and intact alveolar surfaces is also discussed.

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Published In

Langmuir : the ACS journal of surfaces and colloids

DOI

EISSN

1520-5827

ISSN

0743-7463

Publication Date

October 2016

Volume

32

Issue

41

Start / End Page

10570 / 10581

Related Subject Headings

  • Chemical Physics
 

Citation

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ICMJE
MLA
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Parra, E., Kinoshita, K., & Needham, D. (2016). Micropipette Technique Study of Natural and Synthetic Lung Surfactants at the Air-Water Interface: Presence of a SP-B Analog Peptide Promotes Membrane Aggregation, Formation of Tightly Stacked Lamellae, and Growth of Myelin Figures. Langmuir : The ACS Journal of Surfaces and Colloids, 32(41), 10570–10581. https://doi.org/10.1021/acs.langmuir.6b01420
Parra, Elisa, Koji Kinoshita, and David Needham. “Micropipette Technique Study of Natural and Synthetic Lung Surfactants at the Air-Water Interface: Presence of a SP-B Analog Peptide Promotes Membrane Aggregation, Formation of Tightly Stacked Lamellae, and Growth of Myelin Figures.Langmuir : The ACS Journal of Surfaces and Colloids 32, no. 41 (October 2016): 10570–81. https://doi.org/10.1021/acs.langmuir.6b01420.
Parra, Elisa, et al. “Micropipette Technique Study of Natural and Synthetic Lung Surfactants at the Air-Water Interface: Presence of a SP-B Analog Peptide Promotes Membrane Aggregation, Formation of Tightly Stacked Lamellae, and Growth of Myelin Figures.Langmuir : The ACS Journal of Surfaces and Colloids, vol. 32, no. 41, Oct. 2016, pp. 10570–81. Epmc, doi:10.1021/acs.langmuir.6b01420.
Journal cover image

Published In

Langmuir : the ACS journal of surfaces and colloids

DOI

EISSN

1520-5827

ISSN

0743-7463

Publication Date

October 2016

Volume

32

Issue

41

Start / End Page

10570 / 10581

Related Subject Headings

  • Chemical Physics