Título:
|
Divide & Conquer: surfactant protein SP-C and cholesterol modulate phase segregation in lung surfactant
|
Autores:
|
Roldán López, Nuria ;
Pérez Gil, Jesús ;
Morrow, Michael R. ;
García Álvarez, Begoña
|
Tipo de documento:
|
texto impreso
|
Editorial:
|
Elsevier, 2017-08-22
|
Dimensiones:
|
application/pdf
|
Nota general:
|
info:eu-repo/semantics/restrictedAccess
|
Idiomas:
|
|
Palabras clave:
|
Estado = Publicado
,
Materia = Ciencias Biomédicas: Biología: Bioquímica
,
Tipo = Artículo
|
Resumen:
|
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.
|
En línea:
|
https://eprints.ucm.es/46628/1/Roldan%2C%20N.%20et%20al.%202017.%20Divide%20and%20conquer%20surfactant.pdf
|