Topographical Organization of the N-Terminal Segment of Lung Pulmonary Surfactant Protein B (SP-B 1–25) in a Phospholipid Bilayer as Determined by Fluorescence Quenching
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2003/02/01
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Description:The location and depth of each residue on the phospholid bilayer (PB) was determined by fluorescence quenching with synthesized single residue substituted peptides that were rconstituted into DPPC-enriched liposomes. The single residue subsitutions in peptides were either aspartate or tryptophan. Asparate was subsequently labeled with the NCD-4 flurophore. The spin-labeled compounds, 5-DSA, 7-DSA, 12-DSA, CAT-16, and CAT-1 were used in quenching experiments. Our observations indicated that residues 1-6 are located at the surface of PB; residues 7-9 are embedded in PB; residues 10-22 are involved in an amphipathic alpha-helix with its axis somewhat parallel to the surface of PB; residues 23-25 reside at the surface. Effects of the inter-molecule disulfide bond formation in the SP-B 1-25 dimer were also investigated. The data suggest that hydrophobic sides of the amphipathic helixes face each other forming a hydrophobic domain. The environment-sepcific conformational liability in this hydrophobic domain may explain the key impact of SP-B on the phospholipid transport from bi- to mono-layer and in modulating the cell inflammatory response during the respiratory distress syndrome conditions. [Description provided by NIOSH]
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ISSN:0006-3495
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Volume:84
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Issue:2
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NIOSHTIC Number:nn:20027490
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Citation:Biophys J 2003 Feb; 84(2)(Pt 2):54a
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Contact Point Address:1095 Willowdale Road, Morgantown, WV, 26505
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Federal Fiscal Year:2003
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Peer Reviewed:False
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Part Number:2
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Source Full Name:Biophysical Journal
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Main Document Checksum:urn:sha-512:7c6096dbc756ed65b1db0dc46bbb6d3cd8fea075b940410f07f4f4a10613252c0367b546dc299661dadd846c5574755ea323785a7d528bea4b0ed44eb961b96e
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