Abstract
AbstractThe competitive adsorption of lung surfactant (LS) and albumin at the air-liquid interface and the ability of polyethylene glycol (PEG) to mediate LS adsorption are analyzed using pressure area isotherms and grazing incidence x-ray diffraction (GIXD). The addition of albumin drastically reduces the amount of LS on the interface and slightly increases the LS lattice spacing. The addition of PEG restores the characteristic LS peaks, yielding a slightly more compact lattice. The scattering results are consistent with recent work which proposed that albumin creates a physical barrier which eliminates LS adsorption and that PEG enhances LS adsorption but does not significantly change LS surface ordering.
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