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- W1977407430 abstract "Pulmonary surfactant protein B (SP-B) is a hydrophobic 79-residue protein, essential for the respiratory function. SP-B is supposedly involved in the transfer of phospholipid molecules from specific lipid/protein assemblies produced by pneumocytes into the alveolar air-liquid interface to form surface active films competent to stabilize the respiratory surface against collapse along breathing dynamics. Lack of SP-B is lethal, being its absence associated with an irreversible respiratory failure at birth. Quartz crystal microbalance with dissipation technique has been used to analyze SP-B lytic and fusogenic properties in an environment that could be closer to the surfactant multilayer stores thought to be formed beneath pulmonary air-liquid interface. Processes related with unpacking surfactant lipids as they are transferred into the surface and converted into multilayered forms have been attributed to SP-B function although the molecular mechanism by which the protein could perform these actions are entirely unknown. QCM-D technique has been used to characterize how SP-B modulates the adsorption properties to surfaces of DOPC and DPPC membranes containing different physiologically-relevant protein proportions, leading to the formation of membrane stacks on the surface rather than a single supported bilayer. We have also investigated how the collapse of lipid/protein vesicles is affected or modulated by physiologically relevant factors such as lipid composition (i.e. presence of anionic lipids, which increase the effect of SP-B), presence of the other surfactant hydrophobic protein, SP-C, or the addition of Ca2+. These studies have been conducted using both full-length purified porcine SP-B and selected SP-B peptide fragments." @default.
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- W1977407430 date "2009-02-01" @default.
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- W1977407430 title "Study of the Effect Of Pulmonary Surfactant Protein B (SP-B) on Phospholipid Membrane Reorganizations Using Quartz Crystal Microbalances with Dissipation (QCM-D)" @default.
- W1977407430 doi "https://doi.org/10.1016/j.bpj.2008.12.1650" @default.
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