Effects of lung surfactant proteins, SP-B and SP-C, and palmitic acid on monolayer stability

Junqi Ding, Dawn Y. Takamoto, Anja Von Nahmen, Michael M. Lipp, Ka Yee C. Lee, Alan J. Waring, Joseph A. Zasadzinski

Research output: Contribution to journalArticlepeer-review

159 Scopus citations

Abstract

Langmuir isotherms and fluorescence and atomic force microscopy images of synthetic model lung surfactants were used to determine the influence of palmitic acid and synthetic peptides based on the surfactant-specific proteins SP-B and SP-C on the morphology and function of surfactant monolayers. Lung surfactant-specific protein SP-C and peptides based on SP-C eliminate the loss to the subphase of unsaturated lipids necessary for good adsorption and respreading by inducing a transition between monolayers and multilayers within the fluid phase domains of the monolayer. The morphology and thickness of the multilayer phase depends on the lipid composition of the monolayer and the concentration of SP-C or SP-C peptide. Lung surfactant protein SP-B and peptides based on SP-B induce a reversible folding transition at monolayer collapse that allows all components of surfactant to be retained at the interface during respreading. Supplementing Survanta, a clinically used replacement lung surfactant, with a peptide based on the first 25 amino acids of SP-B also induces a similar folding transition at monolayer collapse. Palmitic acid makes the monolayer rigid at low surface tension and fluid at high surface tension and modifies SP-C function. Identifying the function of lung surfactant proteins and lipids is essential to the rational design of replacement surfactants for treatment of respiratory distress syndrome.

Original languageEnglish (US)
Pages (from-to)2262-2272
Number of pages11
JournalBiophysical journal
Volume80
Issue number5
DOIs
StatePublished - 2001
Externally publishedYes

Bibliographical note

Funding Information:
J.D., K.Y.C.L., M.M.L., and J.A.Z. were supported by National Institutes of Health Grant HL-51177; J.A.Z. and A.J.W. were also supported by the Tobacco Related Disease Research Program Grant 8RT-0077. J.D. was supported by Tobacco Related Disease Research Program Grant 8DT-0171. A.J.W. was also supported by National Institutes of Health Grant HL55534, the Drew RCMI Bioinformatics Core (NCRR/RCMI G12 RR 03026), and National Institutes of Health Small Equipment Grant GM 50483. K.Y.C.L. was supported by the March of Dimes Award (5-FY98-0728), the Searle Scholars Program/The Chicago Community Trust (99-C-105), the American Lung Association (RG-085-N), and the Packard Foundation (99-1465).

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