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    Interactions of Spread Lecithin Monolayers with Bovine Serum Albumin in Aqueous Solution

    Year: 1997

    Journal: Langmuir 1997, 13, 4710-4715, 20111221

    Authors: Daechul Cho, Ganesan Narsimhan, and Elias I. Franses

    Organizations: Biochemical and Food Process Engineering, Department of Agricultural and Biological Engineering, Purdue University, West Lafayette, Indiana 47907-1146, and Department of Chemical Engineering, Purdue University, West lafayette, Indiana 47907-1283

    The dynamics of surface pressure (Π) and of surface concentration (Γ) of 14C radiolabeled bovine serum albumin (BSA) adsorbed onto spread lecithin monolayers at the air-water interface were measured. The adsorption of BSA onto spread lecithin monolayers of 107 and 64 Å2/molecule was enhanced at short times (within a few seconds), indicating synergism due to possible dissolution of BSA molecules into loosely or moderately packed lecithin layers. The surface concentration of BSA increased to 2-2.5 mg/m2 from about 1 mg/m2 and the surface pressure to 20-35 mN/m from about 10 mN/m in the presence of spread lecithin monolayer. At long times, monolayer composition was found, however, to be dominated by lecithin. BSA was expelled from the interface by close-packed lecithin monolayers, possibly because of the surface pressure and steric exclusion effects.