Effect of hydrophobic proteins in modulating the mechanical properties of lung surfactant membranes.

Pulmonary surfactant is a membranous complex that enables breathing dynamics at the respiratory surface. Extremely low values of surface tension are achieved at end-expiration thanks to a unique mixture of lipids and proteins. In particular, the hydrophobic surfactant proteins, specially the protein SP-B, are crucial for surfactant biophysical function, in order to provide the surfactant lipid matrix with the ability to form membranous multi-layered interfacial films that sustain optimal mechanical properties.

Studying the interfacial activity and structure of pulmonary surfactant complexes.

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.

Effect of lipid-polymer hybrid nanoparticles on the biophysical function and lateral structure of pulmonary surfactant: Mechanistic in vitro studies.

The interaction between inhaled drug-loaded nanoparticles and pulmonary surfactant (PS) is critical for the efficacy and safety of inhaled nanomedicines. Here, we investigated the effect of small interfering RNA (siRNA)-loaded lipid-polymer hybrid nanoparticles (LPNs), which are designed for treatment of lung inflammation, on the physiological function of PS. By using biophysical in vitro methods we show that siRNA-loaded LPNs affect the biophysical function and lateral structure of PS.

The methylerythritol phosphate pathway as an oxidative stress sense and response system.

The methylerythritol phosphate (MEP) pathway is responsible for biosynthesis of the precursors of isoprenoid compounds in eubacteria and plastids. It is a metabolic alternative to the well-known mevalonate pathway for isoprenoid production found in archaea and eukaryotes. Recently, a role for the MEP pathway in oxidative stress detection, signalling, and response has been identified.