![]() Each SP-B monomer contains three intramolecular disulfide bridges (i.e., Cys-8 to Cys-77, Cys-11 to Cys-71 and Cys-35 to Cys-46). SP-B is a small (79 amino acids monomer MW of 8.7 kDa), lipid-associating protein that is found in the mammalian lung as a covalently linked homodimer, through a disulfide bridge at positions Cys-51, Cys-51′. An important goal of surfactant researchers is to replace animal-derived therapies with fully synthetic preparations based on SP-B and SP-C, produced by recombinant technology or peptide synthesis, and reconstituted with selected synthetic lipids (SL) –. Exogenous surfactant replacement therapies are currently being extended to pediatric and adult patients with direct pulmonary forms of clinical acute lung injury (ALI) and the acute respiratory distress syndrome (ARDS) –. Surfactant therapy using bovine or porcine lung extracts surfactant extracts, which contain only polar lipids and native SP-B and SP-C, has greatly improved the therapeutic outcomes of neonates with respiratory distress (NRDS). Hereditary SP-B deficiency is lethal in humans, while mutations in the SP-C gene may cause interstitial lung disease and increase susceptibility to infection. Despite dipalmitoyl phosphatidylcholine and phosphatidylglycerol constituting its main phospholipid components, the biophysical activity of surfactant in the lung largely depends on the presence of the hydrophobic surfactant protein B (SP-B), and to a lesser degree on the extremely hydrophobic surfactant protein C (SP-C) –. Surfactant is synthesized and secreted into the alveolar fluid by type II cells, and consists of approximately 80% phospholipids, 10% neutral lipids and 10% proteins. Lung surfactant is a complex mixture of lipids (mostly phospholipids) and proteins that is required for normal breathing, due to its ability to reduce alveolar surface tension to very low values. NIH had no role in the design and conduct of the study, in the collection, analysis, and interpretation of the data, and in the preparation, review, or approval of the manuscript.Ĭompeting interests: The authors have declared that no competing interests exist. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.įunding: The authors gratefully acknowledge the financial support of the National Institutes of Health through grants HL-092158, ES-015330, HL-080775, and HL-094641. ![]() Received: JAccepted: DecemPublished: January 13, 2010Ĭopyright: © 2010 Walther et al. ![]() PLoS ONE 5(1):Įditor: Rory Edward Morty, University of Giessen Lung Center, Germany (2010) Critical Structural and Functional Roles for the N-Terminal Insertion Sequence in Surfactant Protein B Analogs. Citation: Walther FJ, Waring AJ, Hernandez-Juviel JM, Gordon LM, Wang Z, Jung C-L, et al. ![]()
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