Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volume 1862, Issue 6, Pages -Publisher
ELSEVIER
DOI: 10.1016/j.bbamem.2020.183216
Keywords
Lung surfactant; Membrane protein; Protein complex; Phospholipid bilayer; Membrane aggregates; FRET
Categories
Funding
- Spanish Ministry of Science, Innovation and Universities [RTI2018-094564-B-I00]
- Regional Government of Madrid [P2018/NMT4389]
- Spanish Ministry of Economy and Competitiveness [BES-2013-066972]
- EMBO shortterm fellowship [7343]
- Portuguese Fundacao para a Ciencia e a Tecnologia (FCT) [007630 UID/QUI/00313/2013, PT2020-PTDC/DTP-FTO/2784/2014]
- FCT (Portugal) [IST -ID/105/2018]
- [FAPESP/20107/2014]
- [PTDC/BIA-BFS/30959/2017]
- Fundação para a Ciência e a Tecnologia [PTDC/BIA-BFS/30959/2017] Funding Source: FCT
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Surfactant protein SP-B is absolutely required for the generation of functional pulmonary surfactant, a unique network of multilayered membranes, which stabilizes the respiratory air-liquid interface. It has been proposed that SP-B assembles into hydrophobic rings and tubes that facilitate the rapid transfer of phospholipids from membrane stores into the interface and the formation of multilayered films, ensuring the stability of the alveoli against physical forces leading to their collapse. To elucidate the molecular organization of SP-B-promoted multilamellar membrane structures, time-resolved Forster Resonance Energy Transfer (FRET) experiments between BODIPY-PC or BODIPY-derivatized SP-B (BODIPY/SP-B), as donor probes, and octadecylrhodamine B, as acceptor probe, were performed in liposomes containing SP-B or BODIPY/SP-B. Our results show that both SP-B and fluorescently labeled SP-B oligomers mediate the connection of adjacent bilayers. Furthermore, by applying rational models to the FRET data, we have been able to provide quantitative details of the structure of SP-B-induced multilayered membrane arrays at the nanometer scale, defining interactions between SP-B rings as key elements for connecting surfactant membranes. The data sustain the structural model and the mechanism of action of SP-B assemblies to sustain the crucial surfactant function.
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