Sequential Adsorption of Human Serum Albumin (HSA), Immunoglobulin G (IgG), and Fibrinogen (Fgn) at HMDSO Plasma Polymer Surfaces

The sequential adsorption of human serum albumin (HSA), immunoglobulin G (IgG), and fibrinogen (Fgn) at hexamethyldisiloxane (HMDSO) plasma polymer surfaces was investigated with ellipsometry and total internal reflection fluorescence spectroscopy (TIRF) as a function of adsorption time, pH, and exc...

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Bibliographic Details
Published in:Journal of colloid and interface science 1997-09, Vol.193 (1), p.88-95
Main Authors: Malmsten, Martin, Muller, Dries, Lassen, Bo
Format: Article
Language:English
Subjects:
Adsorption
Biological and medical sciences
ellipsometry
Fundamental and applied biological sciences. Psychology
Molecular biophysics
plasma polymers
proteins
Surface properties. Adsorption
TIRF
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Summary:The sequential adsorption of human serum albumin (HSA), immunoglobulin G (IgG), and fibrinogen (Fgn) at hexamethyldisiloxane (HMDSO) plasma polymer surfaces was investigated with ellipsometry and total internal reflection fluorescence spectroscopy (TIRF) as a function of adsorption time, pH, and excess electrolyte concentration. HSA was found to self-exchange very slowly (≈ hours) at pH 7.2, irrespective of adsorption time in the range 90 s to 90 min. Preadsorbed HSA was exchanged by Fgn and IgG only to a limited extent irrespectively of pH (5 ≤ pH ≤ 8) and excess electrolyte concentration (5 mM ≤ Cs≤ 150 mM). At an excess electrolyte concentration of 150 mM,the sequential adsorption of Fgn and IgG was dramatically reduced by HSA preadsorption, irrespective of pH. At an excess electrolyte concentration of 5 mM,on the other hand, there were indications of second-layer adsorption of Fgn and IgG.
ISSN:0021-9797
1095-7103
1095-7103
DOI:10.1006/jcis.1997.5039