Phase and Morphology Changes in Lipid Monolayers Induced by SP-B Protein and Its Amino-Terminal Peptide

Both human lung surfactant protein, SP-B, and its amino-terminal peptide, SP-B$_{1-25}$, inhibit the formation of condensed phases in monolayers of palmitic acid, resulting in a new fluid phase. This fluid phase forms a network, separating condensed-phase domains at coexistence. The network persists...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1996-08, Vol.273 (5279), p.1196-1199
Main Authors: Lipp, M. M., Lee, K. Y. C., Zasadzinski, J. A., Waring, A. J.
Format: Article
Language:English
Subjects:
Amino acids
Biochemistry
Biological and medical sciences
Climate
Fatty acids
Fundamental and applied biological sciences. Psychology
Lipids
Lung morphology
Lungs
Microscopy, Fluorescence
Molecular biophysics
Molecules
Networks
Nucleation
Palmitic Acid
Palmitic Acids - chemistry
Peptide Fragments - chemistry
Peptides
Premature Infants
Pressure
Proteins
Proteolipids - chemistry
Pulmonary Surfactants - chemistry
Stripes
Surface areas
Surface Properties
Surface properties. Adsorption
Surfactants
Temperature
Water
Young Children
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Summary:Both human lung surfactant protein, SP-B, and its amino-terminal peptide, SP-B$_{1-25}$, inhibit the formation of condensed phases in monolayers of palmitic acid, resulting in a new fluid phase. This fluid phase forms a network, separating condensed-phase domains at coexistence. The network persists to high surface pressures, altering the nucleation, growth, and morphology of monolayer collapse structures, leading to lower surface tensions on compression and more reversible respreading on expansion. The network is stabilized by the low line tension between the fluid phase and the condensed phase as confirmed by the formation of "stripe" phases.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.273.5279.1196