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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
Affiliation:
Department of Chemistry, The University of Chicago, Chicago, IL 60637, [email protected]
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
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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
Copyright
Copyright © Materials Research Society 2000

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