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   <dc:title>Divide &amp; Conquer: surfactant protein SP-C and cholesterol modulate phase segregation in lung surfactant</dc:title>
   <dc:creator>Roldán López, Nuria</dc:creator>
   <dc:creator>Pérez-Gil, Jesús</dc:creator>
   <dc:creator>Morrow, Michael R.</dc:creator>
   <dc:creator>García Álvarez, Begoña</dc:creator>
   <dc:subject>577.112</dc:subject>
   <dc:subject>Surfactant protein SP-C</dc:subject>
   <dc:subject>Cholesterol</dc:subject>
   <dc:subject>Lung surfactant</dc:subject>
   <dc:subject>Bioquímica (Biología)</dc:subject>
   <dc:subject>2302 Bioquímica</dc:subject>
   <dc:description>Lung surfactant (LS) is an essential system supporting the respiratory function. Cholesterol can be deleterious for LS function, a condition that is reversed by the presence of the lipopeptide SP-C. In this work, the structure of LS-mimicking membranes has been analyzed under the combined effect of SP-C and cholesterol by deuterium NMR and phosphorus NMR and by electron spin resonance. Our results show that SP-C induces phase segregation at 37ºC, resulting in an ordered phase with spectral features resembling an interdigitated state enriched in dipalmitoylphosphatidylcholine, a liquid-crystalline bilayer phase, and an extremely mobile phase consistent with small vesicles or micelles. In the presence of cholesterol, POPC and POPG motion seem to be more hindered by SP-C than dipalmitoylphosphatidylcholine. The use of deuterated cholesterol did not show signs of specific interactions that could be attributed to SP-C or to the other hydrophobic surfactant protein SP-B. Palmitoylation of SP-C had an indirect effect on the extent of protein-lipid perturbations by stabilizing SP-C structure, and seemed to be important to maximize differences among the lipids participating in each phase. These results shed some light on how SP-C-induced lipid perturbations can alter membrane structure to sustain LS functionality at the air-liquid interface.</dc:description>
   <dc:description>Ministerio de Economía y Competitividad (MINECO)</dc:description>
   <dc:description>Comunidad de Madrid</dc:description>
   <dc:description>Ministerio de Educación, Cultura y Deporte (MEC)</dc:description>
   <dc:description>Natural Sciences and Engineering Research Council of Canada</dc:description>
   <dc:description>Sección Deptal. de Bioquímica y Biología Molecular (Biológicas)</dc:description>
   <dc:description>Fac. de Ciencias Biológicas</dc:description>
   <dc:description>TRUE</dc:description>
   <dc:description>pub</dc:description>
   <dc:date>2023-06-17T22:21:40Z</dc:date>
   <dc:date>2023-06-17T22:21:40Z</dc:date>
   <dc:date>2017-08-22</dc:date>
   <dc:type>journal article</dc:type>
   <dc:identifier>https://hdl.handle.net/20.500.14352/18418</dc:identifier>
   <dc:identifier>0006-3495, ESSN: 1542-0086</dc:identifier>
   <dc:identifier>10.1016/j.bpj.2017.06.059</dc:identifier>
   <dc:language>eng</dc:language>
   <dc:relation>(BIO2015-67930-R)</dc:relation>
   <dc:relation>(S2013/ MlT-2807)</dc:relation>
   <dc:rights>restricted access</dc:rights>
   <dc:format>application/pdf</dc:format>
   <dc:publisher>Elsevier</dc:publisher>
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