Sequential Adsorption of Human Serum Albumin (HSA), Immunoglobulin G (IgG), and Fibrinogen (Fgn) at HMDSO Plasma Polymer Surfaces
✍ Scribed by Martin Malmsten; Dries Muller; Bo Lassen
- Publisher
- Elsevier Science
- Year
- 1997
- Tongue
- English
- Weight
- 143 KB
- Volume
- 193
- Category
- Article
- ISSN
- 0021-9797
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✦ Synopsis
The sequential adsorption of human serum albumin (HSA), surface of one protein also enhances the adsorption of other immunoglobulin G (IgG), and fibrinogen (Fgn) at hexamethyldisserum components (2-6, 12-18, 20, 21). One key parameiloxane (HMDSO) plasma polymer surfaces was investigated with ter determining the biological response to an artificial mateellipsometry and total internal reflection fluorescence spectroscopy rial in contact with blood appears to be the adsorbed layer (TIRF) as a function of adsorption time, pH, and excess electrolyte composition. More precisely, preferential adsorption of huconcentration. HSA was found to self-exchange very slowly ( É man serum albumin (HSA) seems to be advantageous for hours) at pH 7.2, irrespective of adsorption time in the range 90 biological acceptance of the material, whereas extensive ads to 90 min. Preadsorbed HSA was exchanged by Fgn and IgG only to a limited extent irrespectively of pH (5 £ pH £ 8) and sorption of, e.g., fibrinogen (Fgn), fibronectin, immunoglobexcess electrolyte concentration (5 m M £ C s £ 150 mM). At an ulin G (IgG), and complement proteins (e.g., C3 and C1q), excess electrolyte concentration of 150 m M, the sequential adsorpappears to be coupled to adverse biological responses such tion of Fgn and IgG was dramatically reduced by HSA preadsorpas increased macrophage uptake and bacterial adhesion (8, tion, irrespective of pH. At an excess electrolyte concentration of 9, 23, 24). 5 mM, on the other hand, there were indications of second-layer Considering this, the quite extensive research effort conadsorption of Fgn and IgG.