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Journal article

Competitive protein adsorption to polymer surface from human serum

From

Polymer Microsystems for Electrophysiology Group, Polymer Micro and Nano Engineering Section, Department of Micro- and Nanotechnology, Technical University of Denmark1

Polymer Micro and Nano Engineering Section, Department of Micro- and Nanotechnology, Technical University of Denmark2

Risø National Laboratory for Sustainable Energy, Technical University of Denmark3

Solar Energy Programme, Risø National Laboratory for Sustainable Energy, Technical University of Denmark4

Polymer Microsystems for Cell Processing Group, Polymer Micro and Nano Engineering Section, Department of Micro- and Nanotechnology, Technical University of Denmark5

Radioecology and Tracer Studies, Radiation Research Division, Risø National Laboratory for Sustainable Energy, Technical University of Denmark6

Radiation Research Division, Risø National Laboratory for Sustainable Energy, Technical University of Denmark7

Surface modification by "soft" plasma polymerisation to obtain a hydrophilic and non-fouling polymer surface has been validated using radioactive labelling. Adsorption to unmodified and modified polymer surfaces, from both single protein and human serum solutions, has been investigated. By using different radioisotopes, albumin and Immunoglobulin G (IgG) adsorption has been monitored simultaneously during competitive adsorption processes, which to our knowledge has not been reported in the literature before.

Results show that albumin and IgG adsorption is dependent on adsorption time and on the presence and concentration of other proteins in bulk solutions during adsorption. Generally, lower albumin and IgG adsorption was observed on the modified and more hydrophilic polymer surfaces, but otherwise the modified and unmodified polymer surfaces showed the same adsorption characteristics.

Language: English
Publisher: Springer US
Year: 2008
Pages: 2179-2185
Journal subtitle: Official Journal of the European Society for Biomaterials
ISSN: 15734838 and 09574530
Types: Journal article
DOI: 10.1007/s10856-007-3318-9
ORCIDs: Larsen, Niels Bent and Hou, Xiaolin

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