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An X-ray diffraction study of alterations in bovine lung surfactant bilayer structures induced by albumin.

Larsson, Marcus LU ; Nylander, Tommy LU ; Keough, Kevin M W and Nag, Kaushik (2006) In Chemistry and Physics of Lipids 144(2). p.137-145
Abstract
Lung surfactant (LS) is an extra-cellular lipid-protein system responsible for maintaining low surface tension in the lung and alveolar stability. Serum proteins cause dysfunction of this material, e.g. in adult respiratory distress syndrome (ARDS). BLES is a clinically used LS consisting of most of the lipids and associated proteins from bovine lung lavage. Aqueous phases of BLES at 30% and 70% hydration, with and without 5% by weight of bovine serum albumin (BSA), calculated on the amount of lipids, were studied using X-ray diffraction during cooling from 42 to 5 degrees C. The diffraction curves are consistent with a transition from a lamellar liquid crystalline phase to a gel phase transition at cooling in the interval 30-20 degrees C.... (More)
Lung surfactant (LS) is an extra-cellular lipid-protein system responsible for maintaining low surface tension in the lung and alveolar stability. Serum proteins cause dysfunction of this material, e.g. in adult respiratory distress syndrome (ARDS). BLES is a clinically used LS consisting of most of the lipids and associated proteins from bovine lung lavage. Aqueous phases of BLES at 30% and 70% hydration, with and without 5% by weight of bovine serum albumin (BSA), calculated on the amount of lipids, were studied using X-ray diffraction during cooling from 42 to 5 degrees C. The diffraction curves are consistent with a transition from a lamellar liquid crystalline phase to a gel phase transition at cooling in the interval 30-20 degrees C. The long-spacings correspond to a reduction of the bilayer thickness during this transition. The wide-angle region shows a peak at 4.1 angstrom below 25 degrees C, which is characteristic of the hexagonal chain packing of the gel phase. The perturbation of the bilayers by the presence of BSA seems to induce a significant decrease of the bilayer thickness. Calculations on the observed limits of swelling (taking place in the range 50-60%) indicate that BSA is closely associated with the BLES bilayers, probably due to electrostatic interaction with the cationic surfactant proteins SP-B and SP-C. This study show that the LS lipid structural organizations are extremely susceptible to small amounts of serum albumin, which may have implications in surfactant related lung disease and clinical applications of surfactant therapy. (c) 2006 Elsevier Ireland Ltd. All rights reserved. (Less)
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author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
lung surfactant, X-ray diffraction, IRDS, ARDS, lung surfactant-albumin interaction, phase transition, bovine lung surfactant extract
in
Chemistry and Physics of Lipids
volume
144
issue
2
pages
137 - 145
publisher
Elsevier
external identifiers
  • wos:000242703900003
  • scopus:33750947315
  • pmid:17055468
ISSN
0009-3084
DOI
10.1016/j.chemphyslip.2006.08.006
language
English
LU publication?
yes
id
c34caef7-b038-42a9-9096-379af971c0ba (old id 162225)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=17055468&dopt=Abstract
date added to LUP
2016-04-01 16:28:38
date last changed
2021-04-13 02:53:51
@article{c34caef7-b038-42a9-9096-379af971c0ba,
  abstract     = {Lung surfactant (LS) is an extra-cellular lipid-protein system responsible for maintaining low surface tension in the lung and alveolar stability. Serum proteins cause dysfunction of this material, e.g. in adult respiratory distress syndrome (ARDS). BLES is a clinically used LS consisting of most of the lipids and associated proteins from bovine lung lavage. Aqueous phases of BLES at 30% and 70% hydration, with and without 5% by weight of bovine serum albumin (BSA), calculated on the amount of lipids, were studied using X-ray diffraction during cooling from 42 to 5 degrees C. The diffraction curves are consistent with a transition from a lamellar liquid crystalline phase to a gel phase transition at cooling in the interval 30-20 degrees C. The long-spacings correspond to a reduction of the bilayer thickness during this transition. The wide-angle region shows a peak at 4.1 angstrom below 25 degrees C, which is characteristic of the hexagonal chain packing of the gel phase. The perturbation of the bilayers by the presence of BSA seems to induce a significant decrease of the bilayer thickness. Calculations on the observed limits of swelling (taking place in the range 50-60%) indicate that BSA is closely associated with the BLES bilayers, probably due to electrostatic interaction with the cationic surfactant proteins SP-B and SP-C. This study show that the LS lipid structural organizations are extremely susceptible to small amounts of serum albumin, which may have implications in surfactant related lung disease and clinical applications of surfactant therapy. (c) 2006 Elsevier Ireland Ltd. All rights reserved.},
  author       = {Larsson, Marcus and Nylander, Tommy and Keough, Kevin M W and Nag, Kaushik},
  issn         = {0009-3084},
  language     = {eng},
  number       = {2},
  pages        = {137--145},
  publisher    = {Elsevier},
  series       = {Chemistry and Physics of Lipids},
  title        = {An X-ray diffraction study of alterations in bovine lung surfactant bilayer structures induced by albumin.},
  url          = {http://dx.doi.org/10.1016/j.chemphyslip.2006.08.006},
  doi          = {10.1016/j.chemphyslip.2006.08.006},
  volume       = {144},
  year         = {2006},
}