Spontaneous formation of interfacial lipid-protein monolayers during adsorption from vesicles.

AUTOR(ES)

Nag, K

RESUMO

Spread and adsorbed monolayers of lipid-protein mixtures have served as models for biomembranes and pulmonary surfactant, but their similarity was unclear. Epifluorescence microscopy of monolayers spontaneously adsorbed from vesicles of dipalmitoylphosphatidylcholine or dipalmitoylphosphatidylcholine plus surfactant protein C (SP-C) showed gas, liquid expanded, and liquid condensed (LC) domains. The shapes and distribution of LC domains in the adsorbed and solvent-spread monolayers were quite similar. Labeled SP-C adsorbed into the air-water interface in the company of the lipids. In both forms of monolayers, SP-C occupied the fluid phase and reduced the size and amount of the LC domains. The properties suggest that these adsorbed and spread monolayers are analogous to one another.

Documentos Relacionados

• Lipid-Protein Interactions in High Density Lipoproteins
• Lipid-protein interaction in the phosphatidylcholine exchange protein.
• Identification and characterization of nonsedimentable lipid-protein microvesicles.
• Membrane Structure: Lipid-Protein Interactions in Microsomal Membranes*
• Preferential solvation and the selectivity of lipid-protein interactions.