Document Detail

Effects of lung surfactant proteins, SP-B and SP-C, and palmitic acid on monolayer stability.
MedLine Citation:
PMID:  11325728     Owner:  NLM     Status:  MEDLINE    
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.
J Ding; D Y Takamoto; A von Nahmen; M M Lipp; K Y Lee; A J Waring; J A Zasadzinski
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biophysical journal     Volume:  80     ISSN:  0006-3495     ISO Abbreviation:  Biophys. J.     Publication Date:  2001 May 
Date Detail:
Created Date:  2001-04-30     Completed Date:  2001-07-26     Revised Date:  2010-09-14    
Medline Journal Info:
Nlm Unique ID:  0370626     Medline TA:  Biophys J     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2262-72     Citation Subset:  IM    
Department of Chemical Engineering, University of California, Santa Barbara, California 93106, USA.
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MeSH Terms
Amino Acid Sequence
Biophysical Phenomena
Chromatography, High Pressure Liquid
Electromagnetic Phenomena
Lung / metabolism*
Membranes, Artificial
Microscopy, Atomic Force
Microscopy, Fluorescence
Molecular Sequence Data
Palmitic Acid / pharmacology*
Peptides / chemistry
Protein Folding
Proteolipids / metabolism*
Pulmonary Surfactants / metabolism*
Surface-Active Agents / chemistry*
Grant Support
Reg. No./Substance:
0/Membranes, Artificial; 0/Peptides; 0/Proteolipids; 0/Pulmonary Surfactants; 0/Surface-Active Agents; 57-10-3/Palmitic Acid

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