Journal article
Fibrinogen adsorption on blocked surface of albumin
Amphiphilic polymers in biological sensing Group, Self-organizing materials for nanotechnology Section, Department of Micro- and Nanotechnology, Technical University of Denmark1
Self-organizing materials for nanotechnology Section, Department of Micro- and Nanotechnology, Technical University of Denmark2
Department of Micro- and Nanotechnology, Technical University of Denmark3
Radioecology and Tracer Studies, Radiation Research Division, Risø National Laboratory for Sustainable Energy, Technical University of Denmark4
Radiation Research Division, Risø National Laboratory for Sustainable Energy, Technical University of Denmark5
Risø National Laboratory for Sustainable Energy, Technical University of Denmark6
We have investigated the adsorption of albumin and fibrinogen onto PET (polyethylene terephthalate) and glass surfaces and how pre-adsorption of albumin onto these surfaces can affect the adsorption of later added fibrinogen. For materials and devices being exposed to blood, adsorption of fibrinogen is often a non-wanted event, since fibrinogen is part of the clotting cascade and unspecific adsorption of fibrinogen can have an influence on the activation of platelets.
Albumin is often used as blocking agent for avoiding unspecific protein adsorption onto surfaces in devices designed to handle biological samples, including protein solutions. It is based on the assumption that proteins adsorbs as a monolayer on surfaces and that proteins do not adsorb on top of each other.
By labelling albumin and fibrinogen with two different radioactive iodine isotopes that emit gamma radiation with different energies, the adsorption of both albumin and fibrinogen has been monitored simultaneously on the same sample. Information about topography and coverage of adsorbed protein layers has been obtained using AFM (Atomic Force Microscopy) analysis in liquid.
Our studies show that albumin adsorbs in a multilayer fashion on PET and that fibrinogen adsorbs on top of albumin when albumin is pre-adsorbed on the surfaces.
Language: | English |
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Year: | 2011 |
Pages: | 71-75 |
ISSN: | 18734367 and 09277765 |
Types: | Journal article |
DOI: | 10.1016/j.colsurfb.2010.12.016 |
ORCIDs: | Hou, Xiaolin |