Hostname: page-component-76fb5796d-45l2p Total loading time: 0 Render date: 2024-04-28T08:15:20.684Z Has data issue: false hasContentIssue false
  • English
  • Français

The Incorporation of Lung Surfactant Specific Protein SP-B Into Lipid Monolayers at the Air-Fluid Interface: A Grazing Incidence x-ray Diffraction Study

Published online by Cambridge University Press:  10 February 2011

K.Y.C. Lee ,
J. Majewski ,
T.L. Kuhl ,
P.B. Howes ,
K. Kjaer ,
M.M. Lipp ,
A.J. Waring ,
J.A. Zasadzinski  and
G.S. Smith
K.Y.C. Lee
Affiliation:
Department of Chemistry, The University of Chicago, Chicago, IL 60637, kayeelee@rainbow.uchicago.edu
J. Majewski
Affiliation:
Manuel Lujan Jr. Neutron Scattering Center, Los Alamos National Laboratory, Los Alamos, NM 87545
T.L. Kuhl
Affiliation:
Department of Chemical Engineering, University of California, Santa Barbara, CA 93106-5080
P.B. Howes
Affiliation:
Condensed Matter Physics and Chemistry Department, Risø National Laboratory, DK-4000, Roskilde, Denmark
K. Kjaer
Affiliation:
Condensed Matter Physics and Chemistry Department, Risø National Laboratory, DK-4000, Roskilde, Denmark
M.M. Lipp
Affiliation:
Department of Chemical Engineering, University of California, Santa Barbara, CA 93106-5080
A.J. Waring
Affiliation:
Department of Pediatrics, Martin Luther King Jr./Drew Medical Center and UCLA, Los Angeles, CA 90095
J.A. Zasadzinski
Affiliation:
Department of Chemical Engineering, University of California, Santa Barbara, CA 93106-5080
G.S. Smith
Affiliation:
Manuel Lujan Jr. Neutron Scattering Center, Los Alamos National Laboratory, Los Alamos, NM 87545
Get access

Abstract

Grazing incidence x-ray diffraction (GIXD) measurements were performed to determine the effects of SP-B1.25, the N-terminus peptide of lung surfactant specific protein SP-B1.25, on the structure of palmitic acid (PA) monolayers. In-plane diffraction shows that the peptide fluidizes a portion of the monolayer, but does not affect the packing of the residual ordered phase. This implies that the peptide resides in the disordered phase, and that the ordered phase is essentially pure lipid. The quantitative insights afforded by this study lead to a better understanding of the lipid/protein interactions found in lung surfactant systems.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 590: Symposium R – Applications of Synchrotron Radiation Techniques…V , 1999 , 177
Copyright
Copyright © Materials Research Society 2000

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

1. Shapiro, D. L. and Notter, R. H., Surfactant Replacement Therapy, Alan R. Liss, New York, 1989.Google Scholar
2. Waring, A., Taeusch, W., Bruni, R., Amirkhanian, J., Fan, B., Stevens, R. and Young, J., Peptide Research 2, p. 308–313 (1989).Google Scholar
3. Takahashi, A., Waring, A., Amirkhanian, J., Fan, B. and Taeusch, W., Biochim. Biophys. Acta 1044, p. 43–49 (1990).10.1016/0005-2760(90)90216-KGoogle Scholar
4. Gordon, L. M., Horvath, S., Longo, M., Zasadzinski, J. A., Taeusch, H. W., Faull, K., Leung, C. and Waring, A. J., Protein Sci. 5, p. 1662–1675 (1996).10.1002/pro.5560050820Google Scholar
5. Lipp, M. M., Lee, K. Y. C., Waring, A. J. and Zasadzinski, J. A., Science 273, p. 1196–1199 (1996).10.1126/science.273.5279.1196Google Scholar
6. Mathialagan, N. and Possmayer, F., Biochiim. Biophys. Acta 1045, p. 121–127 (1990).10.1016/0005-2760(90)90140-SGoogle Scholar
7. Cockshutt, A., Absolom, D. and Possmayer, F., Biochim. Biophys. Acta 1085, p. 248–256 (1991).10.1016/0005-2760(91)90101-MGoogle Scholar
8. Longo, M., Waring, A. and Zasadzinski, J., Biophys. J. 63, p. 760–773 (1992).10.1016/S0006-3495(92)81643-0Google Scholar
9. Longo, M., Bisagno, A. and Zasadzinski, J. A., Science 261, p. 453–456 (1993).10.1126/science.8332910Google Scholar
10. Lipp, M. M., Lee, K. Y. C., Zasadzinski, J. A. and Waring, A. J., Biophys. J. 72, p. 2783–2804 (1997).10.1016/S0006-3495(97)78921-5Google Scholar
11. Als-Nielsen, J. and Kjaer, K. in Phase Transitions in Soft Condensed Matter, edited by Riste, T. and Sherrington, D. (Plenum, New York, 1989), p. 113–138.10.1007/978-1-4613-0551-4_11Google Scholar
12. Majewski, J., Popovitz-Biro, R., Bouwman, W., Kjaer, K., Als-Nielsen, J., Lahav, M. and Leiserowitz, L., Chem. Eur. J. 1, p. 302–309 (1995).10.1002/chem.19950010507Google Scholar
13. Frahm, R., Weigelt, J., Meyer, G. and Materlik, G., Rev. Sci. Instrum. 66, p. 1677–1680 (1995).10.1063/1.1146466Google Scholar
14. Eisenberger, P. and Marra, W. C., Phys. Rev. Lett. 46, p. 1081 (1981).10.1103/PhysRevLett.46.1081Google Scholar
15. Als-Nielsen, J., Jacquemain, D., Kjaer, K., Leveiller, F., Lahav, M. and Leiserowitz, L., Phys. Rep. 246, p. 251–313 (1994).10.1016/0370-1573(94)90046-9Google Scholar
16. Kjaer, K., Physica B 198, p. 100–109 (1994).10.1016/0921-4526(94)90137-6Google Scholar
17. Lipp, M. M., Lee, K. Y. C., Zasadzinski, J. A. and Waring, A. J., Science 273, p. 1196–1199 (1996).10.1126/science.273.5279.1196Google Scholar
18. Jacquemain, D., Leveiller, F., Weinbach, S., Lahav, M., Leiserowitz, L., Kjaer, K. and Als-Nielsen, J., J. Am. Chem. Soc. 113, p. 7684 (1991).10.1021/ja00020a034Google Scholar
19. Kjaer, K., Als-Nielsen, J., Helm, C. A., Tippman-Krayer, P. and Méhwald, H., J. Phys. Chem. 93, p. 3200–3206 (1989).10.1021/j100345a063Google Scholar
20. Lin, B., Shih, M. C., Bohanon, T. M., Ice, G. E. and Dutta, P., Phys. Rev. Lett 65, p. 191–194 (1990).10.1103/PhysRevLett.65.191Google Scholar
21. Kenn, R. M., Béhm, C., Bibo, A. M., Peterson, I. R., Méhwald, H., Als-Nielsen, J. and Kjaer, K., J. Phys. Chem. 95, p. 2092–2097 (1991).10.1021/j100158a034Google Scholar
22. Kaganer, V. M., Méhwald, H. and Dutta, P., Rev. Modern Phys. 71, p. 779–819 (1999).10.1103/RevModPhys.71.779Google Scholar
23. Lee, K. Y. C., Lipp, M. M., Zasadzinski, J. A. and Waring, A. J., Colloids and Surfaces A 28, p. 225–242 (1997).10.1016/S0927-7757(96)03919-2Google Scholar