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RESEARCH PRODUCT
Controllable Nonspecific Protein Adsorption by Charged Hyperbranched Polyglycerol Thin Films
Yaming YuHolger Freysubject
GlycerolPolymersSurface PropertiesAdsorptionMonolayerElectrochemistryOrganic chemistryGeneral Materials ScienceBovine serum albuminSurface plasmon resonance3-Mercaptopropionic AcidSpectroscopychemistry.chemical_classificationbiologyChemistryBilayerCationic polymerizationMembranes ArtificialSerum Albumin BovineSurfaces and InterfacesPolymerSurface Plasmon ResonanceCondensed Matter Physicsbiology.proteinAdsorptionProtein adsorptionNuclear chemistrydescription
Antifouling thin films derived from charged hyperbranched polyglycerol (hbPG) layers were fabricated and evaluated. The anionic hbPG (a-hbPG) monolayers and cationic hbPG/anionic hbPG (c/a-hbPG) bilayers were adsorbed on the underlying self-assembled monolayers (SAMs) of cysteamine and 3-mercaptopropionic acid (3-MPA) by electrostatic interaction, respectively, and their procession was monitored by surface plasmon resonance spectroscopy (SPR). The adsorption of bovine serum albumin (BSA) and fibrinogen on the premade a-hbPG and c/a-hbPG thin films was measured and the capability of these thin films to resist nonspecific protein adsorption was evaluated by SPR as well. It is observed that the c/a-hbPG bilayer films possessed good antifouling properties. With c/a-hbPG bilayers consisting of higher molecular weight a-hbPG, the adsorption of BSA and fibrinogen were as low as 0.015 ng/mm(-2) and 0.0076 ng/mm(-2), respectively, comparable to the traditionally ultralow antifouling surfaces (0.05 ng/mm(-2) of nonspecific protein adsorption). This work proved that the charged hbPG thin films can strongly reduce the nonspecific protein adsorption and have the promise for the antifouling coatings with improved performance.
year | journal | country | edition | language |
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2015-11-13 | Langmuir |