Coating of cobalt chrome substrates with thin films of polar/hydrophobic/ionic polyurethanes: Characterization and interaction with human immunoglobulin G and fibronectin
[Display omitted] •Polar/hydrophobic/ionic polyurethanes (PUs) μm-films are generated on metal.•Organic solvent affects surface structure and chemistry of PUs on cobalt chrome.•Protein adsorption on the PUs films led to a reduced exposure of peptide sequences.•Specific chemistry of the PUs is critic...
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Veröffentlicht in: | Colloids and surfaces, B, Biointerfaces B, Biointerfaces, 2019-07, Vol.179, p.114-120 |
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Sprache: | eng |
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•Polar/hydrophobic/ionic polyurethanes (PUs) μm-films are generated on metal.•Organic solvent affects surface structure and chemistry of PUs on cobalt chrome.•Protein adsorption on the PUs films led to a reduced exposure of peptide sequences.•Specific chemistry of the PUs is critical for biomaterial-protein interactions.
Biomaterial implants often lead to specific tissue reactions that could compromise their bio-integration and/or optimal cellular interactions. Polyurethanes (PU) are of particular interest as coatings to mask CoCr’s bioactivity, since they are generally more biocompatible than metal substrates, present a broad range of chemistry, and have highly tunable-mechanical properties. In the current work, complex polyvinyl-urethanes (referred to as D-PHI materials) are studied for their surface phase structures: specifically, an original D-PHI polymer (O-D-PHI) and a differential formulation with relatively higher hydrophobic and ionic content (HHHI) are of interest. The PUs are diluted in tetrahydrofuran (THF) to generate thin films which differentially influence the physical and chemical properties of the D-PHI coatings. AFM images over time show the gradual appearance of domains exhibiting crystalline organisation, and whose shape and size were dependent on D-PHI thickness (thin films vs non-solvent cast resin materials). After three weeks, a complete stabilization of the crystal state is observed. The thin coatings are stable in an aqueous and 37 °C environment. The adsorption of two human plasmatic proteins Immunoglobulin G (IgG) and Fibronectin (Fn), involved in inflammation and coagulation, was studied. The exposure of specific protein sequences (IgG-Fab, Fn-Cell Binding Domain and Fn-N-terminal domain) were dramatically reduced on both D-PHI materials when compared to bare metal CoCr. The implications of these findings would be relevant to defining coating strategies used to improve the blood clotting and immune cell reactivity to CoCr implant materials. |
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ISSN: | 0927-7765 1873-4367 |
DOI: | 10.1016/j.colsurfb.2019.03.040 |