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Monolayers of immunoglobulin G on polystyrene microparticles and their interactions with human serum albumin
Paulina Żeliszewska1, Monika Wasilewska1, Zbigniew Adamczyk1
1Jerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Science, Niezapominajek 8, PL-30239 Krakow, Poland.
The adsorption of mouse monoclonal immunoglobulin G (IgG) on negatively charged polystyrene microparticles was studied by the laser Doppler velocimetry (LDV) electrophoretic mobility measurements. The dependence of the electrophoretic mobility of microparticles on the IgG concentration in the suspension was determined for different ionic strengths and pHs (3.5, 7.4). The increase in the electrophoretic mobility was quantitatively interpreted in terms of the 3D electrokinetic model. The maximum coverage of IgG on latex was determined by the depletion method aided by AFM imaging. It was shown by monitoring the electrophoretic mobility and hydrodynamic dimeter of IgG covered microparticles over prolonged time periods that IgG adsorption was irreversible. The acid-base properties of the IgG monolayers were also determined in pH cycling experiments. It was also confirmed that the adsorption of human serum albumin (HSA) on saturated IgG monolayers, often referred to as blocking, was negligible at pH 7.4.
The adsorption of mouse monoclonal immunoglobulin G (IgG) on negatively charged polystyrene microparticles was studied by the laser Doppler velocimetry (LDV) electrophoretic mobility measurements. The dependence of the electrophoretic mobility of microparticles on the IgG concentration in the suspension was determined for different ionic strengths and pHs (3.5, 7.4). The increase in the electrophoretic mobility was quantitatively interpreted in terms of the 3D electrokinetic model. The maximum coverage of IgG on latex was determined by the depletion method aided by AFM imaging. It was shown by monitoring the electrophoretic mobility and hydrodynamic dimeter of IgG covered microparticles over prolonged time periods that IgG adsorption was irreversible. The acid-base properties of the IgG monolayers were also determined in pH cycling experiments. It was also confirmed that the adsorption of human serum albumin (HSA) on saturated IgG monolayers, often referred to as blocking, was negligible at pH 7.4.
