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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.

Authors
Wang-Y; Rao-MK; Demchuk-E
Source
Biophys J 2003 Feb; 84(2)(Part 2):54a
Link
NIOSHTIC No.
20027490
Abstract
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.
Keywords
Lung-function; Pulmonary-function; Pulmonary-system; Peptides; Lipids; Phospholipids; Cellular-reactions; Cellular-function
Contact
1095 Willowdale Road, Morgantown, WV, 26505
CODEN
BIOJAU
Publication Date
20030201
Document Type
Abstract
Fiscal Year
2003
NTIS Accession No.
NTIS Price
Issue of Publication
2
ISSN
0006-3495
NIOSH Division
HELD
Source Name
Biophysical Journal
State
WV
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