ArticleBiophysical journal2004
SP-B and SP-C alter diffusion in bilayers of pulmonary surfactant.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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Who cites it
15 citing papers in PubMed, 31 citations in OpenAlex.
- Surfactant Proteins SP-B and SP-C in Pulmonary Surfactant Monolayers: Physical Properties Controlled by Specific Protein-Lipid Interactions.Langmuir : the ACS journal of surfaces and colloids · 2023Article
- Potential Therapeutic Applications of Pulmonary Surfactant Lipids in the Host Defence Against Respiratory Viral Infections.Frontiers in immunology · 2021Review
- Crystallization around solid-like nanosized docks can explain the specificity, diversity, and stability of membrane microdomains.Frontiers in plant science · 2014Article
- The accelerated late adsorption of pulmonary surfactant.Langmuir : the ACS journal of surfaces and colloids · 2011Article
- Combined and independent action of proteins SP-B and SP-C in the surface behavior and mechanical stability of pulmonary surfactant films.Biophysical journal · 2010Article
- Time resolved studies of interfacial reactions of ozone with pulmonary phospholipid surfactants using field induced droplet ionization mass spectrometry.The journal of physical chemistry. B · 2010Article
- Interfacial reactions of ozone with surfactant protein B in a model lung surfactant system.Journal of the American Chemical Society · 2010Article
- Influence of liquid-layer thickness on pulmonary surfactant spreading and collapse.Biophysical journal · 2008Article
- Molecular dynamics simulation study of a pulmonary surfactant film interacting with a carbonaceous nanoparticle.Biophysical journal · 2008Article
- Effects of hydrophobic surfactant proteins on collapse of pulmonary surfactant monolayers.Biophysical journal · 2007Article
- Differential effects of lysophosphatidylcholine on the adsorption of phospholipids to an air/water interface.Biophysical journal · 2007Article
- Effect of surfactant protein A on the physical properties and surface activity of KL4-surfactant.Biophysical journal · 2007Article
- Critical structure-function determinants within the N-terminal region of pulmonary surfactant protein SP-B.Biophysical journal · 2006Article
- Molecular dynamics simulations of the anchoring and tilting of the lung-surfactant peptide SP-B1-25 in palmitic acid monolayers.Biophysical journal · 2005Article
- Effects of gramicidin-A on the adsorption of phospholipids to the air-water interface.Biochimica et biophysica acta · 2005Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The hydrophobic proteins SP-B and SP-C promote rapid adsorption of pulmonary surfactant to an air/water interface by an unknown mechanism. We tested the hypothesis that these proteins accelerate adsorption by disrupting the structure of the lipid bilayer, either by a generalized increase in fluidity or by a focal induction of interfacial boundaries within the bilayer. We used fluorescence recovery after photobleaching to measure diffusion of nitrobenzoxadiazolyl-dimyristoyl-phosphatidylethanolamine between 11 and 54 degrees C in multilayers containing the complete set of lipids and proteins in calf lung surfactant extract (CLSE), or the complete set of neutral and phospholipids without the proteins. Above 35 degrees C, Arrhenius plots of diffusion were parallel for CLSE and neutral and phospholipids, but shifted to lower values for CLSE, suggesting that the proteins rigidify the lipid bilayer rather than producing the proposed increase in membrane fluidity. The slopes of the Arrhenius plots for CLSE were steeper below 35 degrees C, suggesting that the proteins induce phase separation at that temperature. The mobile fraction fell below 27 degrees C, consistent with a percolation threshold of coexisting gel and liquid-crystal phases. The induction of lateral phase separation in CLSE, however, does not correlate with apparent changes in adsorption kinetics at this temperature. Our results suggest that SP-B and SP-C accelerate adsorption through a mechanism other than the disruption of surfactant bilayers, possibly by stabilizing a high-energy, highly curved adsorption intermediate.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.