ArticleThe journal of physical chemistry. B2020
Location of the Hydrophobic Surfactant Proteins, SP-B and SP-C, in Fluid-Phase Bilayers.
Article in The journal of physical chemistry. B, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 22 citations in OpenAlex.
- Effects of an alkane on the adsorption and collapse by the lipids of pulmonary surfactant.Biophysical journal · 2026Article
- Intra- and extrapulmonary lipopolysaccharides-induced acute lung injury and pharmacotherapeutic response patterns in ventilated 7-day-old rabbits.Experimental biology and medicine (Maywood, N.J.) · 2026Article
- Conformational changes of surfactant protein B due to the alveolar air/liquid interface using molecular dynamics.Journal of molecular modeling · 2025Article
- Effects of spontaneous curvature on interfacial adsorption and collapse of phospholipid monolayers.American journal of physiology. Lung cellular and molecular physiology · 2024Article
- The biophysical function of pulmonary surfactant.Biophysical journal · 2024Review
- 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
- Antimicrobial Peptide Mechanism Studied by Scattering-Guided Molecular Dynamics Simulation.The journal of physical chemistry. B · 2022Article
- Suppression of LBiophysical journal · 2021Article
- Guardians of the Cell: State-of-the-Art of Membrane Proteins from a Computational Point-of-View.Methods in molecular biology (Clifton, N.J.) · 2021Article
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Authors and funding
11 authors at 3 institutions in 3 countries.
Funding
Abstract
The hydrophobic surfactant proteins, SP-B and SP-C, promote rapid adsorption by the surfactant lipids to the surface of the liquid that lines the alveolar air sacks of the lungs. To gain insights into the mechanisms of their function, we used X-ray diffuse scattering (XDS) and molecular dynamics (MD) simulations to determine the location of SP-B and SP-C within phospholipid bilayers. Initial samples contained the surfactant lipids from extracted calf surfactant with increasing doses of the proteins. XDS located protein density near the phospholipid headgroup and in the hydrocarbon core, presumed to be SP-B and SP-C, respectively. Measurements on dioleoylphosphatidylcholine (DOPC) with the proteins produced similar results. MD simulations of the proteins with DOPC provided molecular detail and allowed direct comparison of the experimental and simulated results. Simulations used conformations of SP-B based on other members of the saposin-like family, which form either open or closed V-shaped structures. For SP-C, the amino acid sequence suggests a partial α-helix. Simulations fit best with measurements of XDS for closed SP-B, which occurred at the membrane surface, and SP-C oriented along the hydrophobic interior. Our results provide the most definitive evidence yet concerning the location and orientation of the hydrophobic surfactant proteins.
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