ArticleBiochimica et biophysica acta2005
Effects of gramicidin-A on the adsorption of phospholipids to the air-water interface.
Article in Biochimica et biophysica acta, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 30 citations in OpenAlex.
- Effects of an alkane on the adsorption and collapse by the lipids of pulmonary surfactant.Biophysical journal · 2026Article
- 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
- Changes in membrane elasticity caused by the hydrophobic surfactant proteins correlate poorly with adsorption of lipid vesicles.Soft matter · 2021Article
- Suppression of LBiophysical journal · 2021Article
- Location of the Hydrophobic Surfactant Proteins, SP-B and SP-C, in Fluid-Phase Bilayers.The journal of physical chemistry. B · 2020Article
- The LLangmuir : the ACS journal of surfaces and colloids · 2018Article
- Hydrophobic surfactant proteins strongly induce negative curvature.Biophysical journal · 2015Article
- An anionic phospholipid enables the hydrophobic surfactant proteins to alter spontaneous curvature.Biophysical journal · 2013Article
- Reconstitution of membrane proteins into model membranes: seeking better ways to retain protein activities.International journal of molecular sciences · 2013Review
- Differential effects of the hydrophobic surfactant proteins on the formation of inverse bicontinuous cubic phases.Langmuir : the ACS journal of surfaces and colloids · 2012Article
- The accelerated late adsorption of pulmonary surfactant.Langmuir : the ACS journal of surfaces and colloids · 2011Article
- Hydrophobic surfactant proteins induce a phosphatidylethanolamine to form cubic phases.Biophysical journal · 2010Article
- The biophysical function of pulmonary surfactant.Respiratory physiology & neurobiology · 2008Review
- 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
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Prior studies suggest that the hydrophobic surfactant proteins, SP-B and SP-C, promote adsorption of the lipids in pulmonary surfactant to an air-water interface by stabilizing a negatively curved rate-limiting structure that is intermediate between bilayer vesicles and the surface film. This model predicts that other peptides capable of stabilizing negative curvature should also promote lipid adsorption. Previous reports have shown that under appropriate conditions, gramicidin-A (GrA) induces dioleoyl phosphatidylcholine (DOPC), but not dimyristoyl phosphatidylcholine (DMPC), to form the negatively curved hexagonal-II (H(II)) phase. The studies reported here determined if GrA would produce the same effects on adsorption of DMPC and DOPC that the hydrophobic surfactant proteins have on the surfactant lipids. Small angle X-ray scattering and (31)P-nuclear magnetic resonance confirmed that at the particular conditions used to study adsorption, GrA induced DOPC to form the H(II) phase, but DMPC remained lamellar. Measurements of surface tension showed that GrA in vesicles produced a general increase in the rate of adsorption for both phospholipids. When restricted to the interface, however, in preexisting films, GrA with DOPC, but not with DMPC, replicated the ability of the surfactant proteins to promote adsorption of vesicles containing only the lipids. The correlation between the structural and functional effects of GrA with the two phospholipids, and the similar effects on adsorption of GrA with DOPC and the hydrophobic surfactant proteins with the surfactant lipids fit with the model in which SP-B and SP-C facilitate adsorption by stabilizing a rate-limiting intermediate with negative curvature.
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Registered trials
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