RT Journal Article
T1 Studying the interfacial activity and structure of pulmonary surfactant complexes
A1 Collada Marugán, Ainhoa
A1 Cruz Rodríguez, Antonio
A1 Pérez Gil, Jesús
AB Pulmonary surfactant (PS) is a membranous complex that coats the respiratory air-liquid interface in air-breathing animal lungs. Its main function is to minimize the surface tension at the end of expiration, what is needed for preventing alveolar collapse. Although the tension reduction capabilities of surfactant depend on the formation of air-exposed phospholipid-enriched monolayers, the interfacial surfactant films are far from simple monolayers. Surfactant surface films are dynamically interconnected to continuously secreted newly synthetized material thanks to the action of a pair of very hydrophobic proteins, termed SP-B and SP-C, which are responsible to modulate the biophysical behavior of the complex. Other proteins in the system, such as the hydrophilic SP-A and SP-D, are integrated into different surfactant structures but participate primarily in the immune defense of the lung. In spite of countless studies on the structure and chemico-physical properties of surfactant membranes, the full complexity of surfactant three-dimensional structure is far from being completely understood. Here we review some of the most useful techniques that have allowed the characterization of the PS system along the years to develop the current models interpreting surfactant structure-function relationships.
PB Elsevier
SN 0009-3084
YR 2024
FD 2024-11-23
LK https://hdl.handle.net/20.500.14352/117233
UL https://hdl.handle.net/20.500.14352/117233
LA eng
NO Collada, A., Cruz, A., & Pérez-Gil, J. (2025). Studying the interfacial activity and structure of pulmonary surfactant complexes. Chemistry and Physics of Lipids, 266, 105459. https://doi.org/10.1016/j.chemphyslip.2024.105459
NO The authors acknowledge funding from the Spanish Ministry of Science and Innovation (PID2021-124932OB-100).
NO Ministerio de Ciencia e Innovación (España)
DS Docta Complutense
RD 10 abr 2025