| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
Biophys J, May 2001, p. 2262-2272, Vol. 80, No. 5

and
*Department of Chemical Engineering, University of California,
Santa Barbara, California 93106;
Department of Chemistry,
University of Chicago, Chicago, Illinois 60637; and
Department of Pediatrics, University of California, Los
Angeles, California 90059 USA
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.
Biophys J, May 2001, p. 2262-2272, Vol. 80, No. 5
© 2001 by the Biophysical Society 0006-3495/01/05/2262/11 $2.00
This article has been cited by other articles:
![]() |
Y. Y. Zuo, E. Keating, L. Zhao, S. M. Tadayyon, R. A. W. Veldhuizen, N. O. Petersen, and F. Possmayer Atomic Force Microscopy Studies of Functional and Dysfunctional Pulmonary Surfactant Films. I. Micro- and Nanostructures of Functional Pulmonary Surfactant Films and the Effect of SP-A Biophys. J., May 1, 2008; 94(9): 3549 - 3564. [Abstract] [Full Text] [PDF] |
||||
![]() |
F. Lhert, W. Yan, S. C. Biswas, and S. B. Hall Effects of Hydrophobic Surfactant Proteins on Collapse of Pulmonary Surfactant Monolayers Biophys. J., December 15, 2007; 93(12): 4237 - 4243. [Abstract] [Full Text] [PDF] |
||||
![]() |
P. C. Stenger and J. A. Zasadzinski Enhanced Surfactant Adsorption via Polymer Depletion Forces: A Simple Model for Reversing Surfactant Inhibition in Acute Respiratory Distress Syndrome Biophys. J., January 1, 2007; 92(1): 3 - 9. [Abstract] [Full Text] [PDF] |
||||
![]() |
F. Gerber, M. P. Krafft, T. F. Vandamme, M. Goldmann, and P. Fontaine Fluidization of a Dipalmitoyl Phosphatidylcholine Monolayer by Fluorocarbon Gases: Potential Use in Lung Surfactant Therapy Biophys. J., May 1, 2006; 90(9): 3184 - 3192. [Abstract] [Full Text] [PDF] |
||||
![]() |
H. W. Taeusch, J. B. de la Serna, J. Perez-Gil, C. Alonso, and J. A. Zasadzinski Inactivation of Pulmonary Surfactant Due to Serum-Inhibited Adsorption and Reversal by Hydrophilic Polymers: Experimental Biophys. J., September 1, 2005; 89(3): 1769 - 1779. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. A. Zasadzinski, T. F. Alig, C. Alonso, J. B. de la Serna, J. Perez-Gil, and H. W. Taeusch Inhibition of Pulmonary Surfactant Adsorption by Serum and the Mechanisms of Reversal by Hydrophilic Polymers: Theory Biophys. J., September 1, 2005; 89(3): 1621 - 1629. [Abstract] [Full Text] [PDF] |
||||
![]() |
C. Alonso, A. Waring, and J. A. Zasadzinski Keeping Lung Surfactant Where It Belongs: Protein Regulation of Two-Dimensional Viscosity Biophys. J., July 1, 2005; 89(1): 266 - 273. [Abstract] [Full Text] [PDF] |
||||
![]() |
C. G. Cochrane Pulmonary surfactant in allergic inflammation: new insights into the molecular mechanisms of surfactant function Am J Physiol Lung Cell Mol Physiol, April 1, 2005; 288(4): L608 - L609. [Full Text] [PDF] |
||||
![]() |
C. Alonso, T. Alig, J. Yoon, F. Bringezu, H. Warriner, and J. A. Zasadzinski More Than a Monolayer: Relating Lung Surfactant Structure and Mechanics to Composition Biophys. J., December 1, 2004; 87(6): 4188 - 4202. [Abstract] [Full Text] [PDF] |
||||
![]() |
T. F. Alig, H. E. Warriner, L. Lee, and J. A. Zasadzinski Electrostatic Barrier to Recovery of Dipalmitoylphosphatidylglycerol Monolayers after Collapse Biophys. J., February 1, 2004; 86(2): 897 - 904. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. Cruz, L. Vazquez, M. Velez, and J. Perez-Gil Effect of Pulmonary Surfactant Protein SP-B on the Micro- and Nanostructure of Phospholipid Films Biophys. J., January 1, 2004; 86(1): 308 - 320. [Abstract] [Full Text] [PDF] |
||||
![]() |
C. R. Flach, P. Cai, D. Dieudonne, J. W. Brauner, K. M. W. Keough, J. Stewart, and R. Mendelsohn Location of Structural Transitions in an Isotopically Labeled Lung Surfactant SP-B Peptide by IRRAS Biophys. J., July 1, 2003; 85(1): 340 - 349. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. A. Freites, Y. Choi, and D. J. Tobias Molecular Dynamics Simulations of a Pulmonary Surfactant Protein B Peptide in a Lipid Monolayer Biophys. J., April 1, 2003; 84(4): 2169 - 2180. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. M. Brockman, Z. Wang, R. H. Notter, and R. A. Dluhy Effect of Hydrophobic Surfactant Proteins SP-B and SP-C on Binary Phospholipid Monolayers: II. Infrared External Reflectance-Absorption Spectroscopy Biophys. J., January 1, 2003; 84(1): 326 - 340. [Abstract] [Full Text] [PDF] |
||||
![]() |
S. Shanmukh, P. Howell, J. E. Baatz, and R. A. Dluhy Effect of Hydrophobic Surfactant Proteins SP-B and SP-C on Phospholipid Monolayers. Protein Structure Studied Using 2D IR and beta nu Correlation Analysis Biophys. J., October 1, 2002; 83(4): 2126 - 2141. [Abstract] [Full Text] [PDF] |
||||
![]() |
D. Knebel, M. Sieber, R. Reichelt, H.-J. Galla, and M. Amrein Fluorescence Light Microscopy of Pulmonary Surfactant at the Air-Water Interface of an Air Bubble of Adjustable Size Biophys. J., July 1, 2002; 83(1): 547 - 555. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. Ikegami, T. E. Weaver, J. J. Conkright, P. D. Sly, G. F. Ross, J. A. Whitsett, and S. W. Glasser Deficiency of SP-B reveals protective role of SP-C during oxygen lung injury J Appl Physiol, February 1, 2002; 92(2): 519 - 526. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |