Effect of surface charge on adsorption of bovine serum albumin as studied by ellipsometry 1. Adsorption on cationic monolayer |
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Authors: | N. Watanabe T. Shirakawa M. Iwahashi K. Ohbu T. Seimiya |
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Affiliation: | (1) Present address: Department of Chemistry, Faculty of Science, Tokyo Metropolitan University, Tokyo, Japan;(2) Department of Chemistry, Faculty of Hygienic Science, Kitasato University, Kanagawa, Japan;(3) Applied Research Laboratories II, Lion Corporation, Tokyo, Japan |
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Abstract: | ![]() The adsorption of bovine serum albumin (BSA) onto a cationic monolayer (N,N-dimethyl-N,N-dialkylammonium chloride) spread at the air/water interface was studied by ellipsometry. Both thicknesses and refractive indices of the BSA layer adsorbed at the monolayer/solution interface are estimated from the observed change in phase difference and the ratio of reflection coefficients. The amount of adsorption of BSA resembles a Langmuir type isotherm. The adsorption changes with pH asymmetrically with respect to the pH of maximum adsorption, which was calculated to be 5.06 ± 0.47 mg/m2. The amount of maximum adsorption implies that the BSA molecule adsorbs to the surface in a mode intermediate between side-on and end-on . |
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Keywords: | Ellipsometry bovine serum albumin protein adsorption cationic monolayer |
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