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Environmental Pollutant Ozone Causes Damage to Lung Surfactant Protein B (SP-B)
Univ London, Dept Biol Sci, Birkbeck Coll, London WC1E 7HX, England.;Univ London, Inst Struct & Mol Biol, Birkbeck Coll, London WC1E 7HX, England..
Univ London, Dept Biol Sci, Birkbeck Coll, London WC1E 7HX, England.;Univ London, Inst Struct & Mol Biol, Birkbeck Coll, London WC1E 7HX, England..
Uppsala University, Disciplinary Domain of Science and Technology, Physics, Department of Physics and Astronomy, Materials Physics.
Univ London, Dept Biol Sci, Birkbeck Coll, London WC1E 7HX, England.;Univ London, Inst Struct & Mol Biol, Birkbeck Coll, London WC1E 7HX, England..
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2015 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 54, no 33, 5185-5197 p.Article in journal (Refereed) Published
Abstract [en]

Lung surfactant protein B (SP-B) is an essential protein found in the surfactant fluid at the air water interface of the lung. Exposure to the air pollutant ozone could potentially damage SP-B and lead to respiratory distress. We have studied two peptides, one consisting of the N-terminus of SP-B [SP-B(1-25)] and the other a construct of the N- and C-termini of SP-B [SP-B-(1-25,B-63-78)], called SMB. Exposure to dilute levels of ozone (similar to 2 ppm) of monolayers of each peptide at the air water interface leads to a rapid reaction, which is evident from an increase in the surface tension. Fluorescence experiments revealed that this increase in surface tension is accompanied by a loss of fluorescence from the tryptophan residue at the interface. Neutron and X-ray reflectivity experiments show that, in contrast to suggestions in the literature, the peptides are not solubilized upon oxidation but rather remain at the interface with little change in their hydration. Analysis of the product material reveals that no cleavage of the peptides occurs, but a more hydrophobic product is slowly formed together with an increased level of oligomerization. We attributed this to partial unfolding of the peptides. Experiments conducted in the presence of phospholipids reveal that the presence of the lipids does not prevent oxidation of the peptides. Our results strongly suggest that exposure to low levels of ozone gas will damage SP-B, leading to a change in its structure. The implication is that the oxidized protein will be impaired in its ability to interact at the air water interface with negatively charged phosphoglycerol lipids, thus compromising what is thought to be its main biological function.

Place, publisher, year, edition, pages
2015. Vol. 54, no 33, 5185-5197 p.
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
URN: urn:nbn:se:uu:diva-262983DOI: 10.1021/acs.biochem.5b00308ISI: 000360324300008PubMedID: 26270023OAI: oai:DiVA.org:uu-262983DiVA: diva2:856160
Funder
Wellcome trust, 093468/Z/10/Z
Available from: 2015-09-23 Created: 2015-09-23 Last updated: 2017-12-01Bibliographically approved

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Rennie, Adrian R.

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