Synchrotron X-Ray Study of Lung Surfactant-Specific Protein SP-B in Lipid Monolayers
This work reports the first x-ray scattering measurements to determine the effects of SP-B 1–25, the N-terminus peptide of lung surfactant-specific protein SP-B, on the structure of palmitic acid (PA) monolayers. In-plane diffraction shows that the peptide fluidizes a portion of the monolayer but do...
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| Veröffentlicht in: | Biophysical journal 2001-07, Vol.81 (1), p.572-585 |
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| creator | Lee, Ka Yee C. Majewski, Jaroslaw Kuhl, Tonya L. Howes, Paul B. Kjaer, Kristian Lipp, Michael M. Waring, Alan J. Zasadzinski, Joseph A. Smith, Greg S. |
| description | This work reports the first x-ray scattering measurements to determine the effects of SP-B
1–25, the N-terminus peptide of lung surfactant-specific protein SP-B, 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, in agreement with fluorescence microscopy studies. X-ray reflectivity shows that the peptide is oriented in the lipid monolayer at an angle of ∼56° relative to the interface normal, with one end protruding past the hydrophilic region into the fluid subphase and the other end embedded in the hydrophobic region of the monolayer. The quantitative insights afforded by this study lead to a better understanding of the lipid/protein interactions found in lung surfactant systems. |
| doi_str_mv | 10.1016/S0006-3495(01)75724-4 |
| format | Article |
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1–25, the N-terminus peptide of lung surfactant-specific protein SP-B, 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, in agreement with fluorescence microscopy studies. X-ray reflectivity shows that the peptide is oriented in the lipid monolayer at an angle of ∼56° relative to the interface normal, with one end protruding past the hydrophilic region into the fluid subphase and the other end embedded in the hydrophobic region of the monolayer. The quantitative insights afforded by this study lead to a better understanding of the lipid/protein interactions found in lung surfactant systems.</description><identifier>ISSN: 0006-3495</identifier><identifier>EISSN: 1542-0086</identifier><identifier>DOI: 10.1016/S0006-3495(01)75724-4</identifier><identifier>PMID: 11423439</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Biology ; Lipid Metabolism ; Lipids ; Lungs ; Membranes, Artificial ; Molecular Conformation ; Molecular Sequence Data ; Palmitic Acid - metabolism ; Peptides ; Physics ; Protein Structure, Tertiary ; Proteins ; Proteolipids - chemistry ; Proteolipids - metabolism ; Pulmonary Surfactants - chemistry ; Pulmonary Surfactants - metabolism ; Sodium Chloride - metabolism ; Synchrotrons ; Temperature ; Water - metabolism ; X-Ray Diffraction - instrumentation ; X-Ray Diffraction - methods ; X-rays</subject><ispartof>Biophysical journal, 2001-07, Vol.81 (1), p.572-585</ispartof><rights>2001 The Biophysical Society</rights><rights>Copyright Biophysical Society Jul 2001</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c556t-3d744d3a48abf2e8124e2e1cdb7992344ee51b1bb0bda884a986e4d5d3168b4b3</citedby><cites>FETCH-LOGICAL-c556t-3d744d3a48abf2e8124e2e1cdb7992344ee51b1bb0bda884a986e4d5d3168b4b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1301536/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006349501757244$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,3537,27901,27902,53766,53768,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11423439$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lee, Ka Yee C.</creatorcontrib><creatorcontrib>Majewski, Jaroslaw</creatorcontrib><creatorcontrib>Kuhl, Tonya L.</creatorcontrib><creatorcontrib>Howes, Paul B.</creatorcontrib><creatorcontrib>Kjaer, Kristian</creatorcontrib><creatorcontrib>Lipp, Michael M.</creatorcontrib><creatorcontrib>Waring, Alan J.</creatorcontrib><creatorcontrib>Zasadzinski, Joseph A.</creatorcontrib><creatorcontrib>Smith, Greg S.</creatorcontrib><title>Synchrotron X-Ray Study of Lung Surfactant-Specific Protein SP-B in Lipid Monolayers</title><title>Biophysical journal</title><addtitle>Biophys J</addtitle><description>This work reports the first x-ray scattering measurements to determine the effects of SP-B
1–25, the N-terminus peptide of lung surfactant-specific protein SP-B, 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, in agreement with fluorescence microscopy studies. X-ray reflectivity shows that the peptide is oriented in the lipid monolayer at an angle of ∼56° relative to the interface normal, with one end protruding past the hydrophilic region into the fluid subphase and the other end embedded in the hydrophobic region of the monolayer. The quantitative insights afforded by this study lead to a better understanding of the lipid/protein interactions found in lung surfactant systems.</description><subject>Amino Acid Sequence</subject><subject>Biology</subject><subject>Lipid Metabolism</subject><subject>Lipids</subject><subject>Lungs</subject><subject>Membranes, Artificial</subject><subject>Molecular Conformation</subject><subject>Molecular Sequence Data</subject><subject>Palmitic Acid - metabolism</subject><subject>Peptides</subject><subject>Physics</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Proteolipids - chemistry</subject><subject>Proteolipids - metabolism</subject><subject>Pulmonary Surfactants - chemistry</subject><subject>Pulmonary Surfactants - metabolism</subject><subject>Sodium Chloride - metabolism</subject><subject>Synchrotrons</subject><subject>Temperature</subject><subject>Water - metabolism</subject><subject>X-Ray Diffraction - instrumentation</subject><subject>X-Ray Diffraction - 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metabolism</topic><topic>Peptides</topic><topic>Physics</topic><topic>Protein Structure, Tertiary</topic><topic>Proteins</topic><topic>Proteolipids - chemistry</topic><topic>Proteolipids - metabolism</topic><topic>Pulmonary Surfactants - chemistry</topic><topic>Pulmonary Surfactants - metabolism</topic><topic>Sodium Chloride - metabolism</topic><topic>Synchrotrons</topic><topic>Temperature</topic><topic>Water - metabolism</topic><topic>X-Ray Diffraction - instrumentation</topic><topic>X-Ray Diffraction - methods</topic><topic>X-rays</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lee, Ka Yee C.</creatorcontrib><creatorcontrib>Majewski, Jaroslaw</creatorcontrib><creatorcontrib>Kuhl, Tonya L.</creatorcontrib><creatorcontrib>Howes, Paul B.</creatorcontrib><creatorcontrib>Kjaer, Kristian</creatorcontrib><creatorcontrib>Lipp, Michael M.</creatorcontrib><creatorcontrib>Waring, Alan J.</creatorcontrib><creatorcontrib>Zasadzinski, Joseph A.</creatorcontrib><creatorcontrib>Smith, Greg S.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>SIRS Editorial</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biophysical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lee, Ka Yee C.</au><au>Majewski, Jaroslaw</au><au>Kuhl, Tonya L.</au><au>Howes, Paul B.</au><au>Kjaer, Kristian</au><au>Lipp, Michael M.</au><au>Waring, Alan J.</au><au>Zasadzinski, Joseph A.</au><au>Smith, Greg S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Synchrotron X-Ray Study of Lung Surfactant-Specific Protein SP-B in Lipid Monolayers</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>2001-07-01</date><risdate>2001</risdate><volume>81</volume><issue>1</issue><spage>572</spage><epage>585</epage><pages>572-585</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><abstract>This work reports the first x-ray scattering measurements to determine the effects of SP-B
1–25, the N-terminus peptide of lung surfactant-specific protein SP-B, 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, in agreement with fluorescence microscopy studies. X-ray reflectivity shows that the peptide is oriented in the lipid monolayer at an angle of ∼56° relative to the interface normal, with one end protruding past the hydrophilic region into the fluid subphase and the other end embedded in the hydrophobic region of the monolayer. The quantitative insights afforded by this study lead to a better understanding of the lipid/protein interactions found in lung surfactant systems.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>11423439</pmid><doi>10.1016/S0006-3495(01)75724-4</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Biophysical journal, 2001-07, Vol.81 (1), p.572-585 |
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| source | MEDLINE; Cell Press Free Archives; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | Amino Acid Sequence Biology Lipid Metabolism Lipids Lungs Membranes, Artificial Molecular Conformation Molecular Sequence Data Palmitic Acid - metabolism Peptides Physics Protein Structure, Tertiary Proteins Proteolipids - chemistry Proteolipids - metabolism Pulmonary Surfactants - chemistry Pulmonary Surfactants - metabolism Sodium Chloride - metabolism Synchrotrons Temperature Water - metabolism X-Ray Diffraction - instrumentation X-Ray Diffraction - methods X-rays |
| title | Synchrotron X-Ray Study of Lung Surfactant-Specific Protein SP-B in Lipid Monolayers |
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