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. 2019 Dec 16;2:470. doi: 10.1038/s42003-019-0662-5

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 9 — Lung surfactant was labeled with a trace of fluorescent Alexa488-labeled surfactant protein SP-B (F-SP-B, 1% (w/w) with respect to lipids) and with rhodamine-DOPE (0.1% mol/mol probe/phospholipid) in the presence or absence of purified NETs. The surfactant was then applied onto the air-water interface of a Langmuir surface balance and the films formed were compressed to a surface pressure of 30 mN/m. The compressed films were finally transferred to glass cover slips and analyzed under the epifluorescence microscope. a In the absence of NETs (control), compressed lung surfactant films segregate probe-excluding highly-packed domains enriched in saturated phospholipids, which are necessary to reach the lowest surface tensions. b In the presence of NETs, condensed phospholipid domains are not observed, being the structure and lateral packing of the lung surfactant film severely impaired. Scale bar, 25 μm.