Preparation of a beta-tricalcium phosphate nanocoating and its protein adsorption behaviour by quartz crystal microbalance with dissipation technique
[Display omitted] •A method to prepare the beta-tricalcium phosphate (β-TCP) nanocoating is provided.•The β-TCP nanocoating could be used in quartz crystal microbalance with dissipation.•Investigate the adsorption behaviour of different proteins on the β-TCP and Au surfaces.•Deepen the understanding...
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Veröffentlicht in: | Colloids and surfaces, B, Biointerfaces B, Biointerfaces, 2018-02, Vol.162, p.1-7 |
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Format: | Artikel |
Sprache: | eng |
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•A method to prepare the beta-tricalcium phosphate (β-TCP) nanocoating is provided.•The β-TCP nanocoating could be used in quartz crystal microbalance with dissipation.•Investigate the adsorption behaviour of different proteins on the β-TCP and Au surfaces.•Deepen the understanding of the interactions between biomaterials and proteins.
Beta-tricalcium phosphate (β-TCP) nanocoatings, which can be analysed using a quartz crystal microbalance with dissipation technique (QCM-D), were fabricated on a gold surface by electrophoretic deposition. The influences of electric field intensity and electrophoresis time were investigated. The adsorption behaviours of bovine serum albumin (BSA) and lysozyme (LSZ) on Au and β-TCP surfaces were observed in real time by QCM-D. The homogeneous β-TCP nanocoating with moderately sized particles on gold surface was fabricated at 25V/cm for 5min, and it met the requirements for the QCM-D experiment. The adsorption behaviour of BSA was different from that of LSZ, which was caused by the differences of protein properties. The adsorption quantity of BSA on a β-TCP surface was higher than that on a gold surface. However, the adsorption amount of LSZ on a β-TCP surface was lower than that on a gold surface. The electrostatic force was the major factor affecting the adsorption quantities of BSA and LSZ on Au and β-TCP surfaces based on the investigation of various factors. The findings reported here will be useful for understanding the mechanism of the interaction between biomaterials and proteins. |
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ISSN: | 0927-7765 1873-4367 |
DOI: | 10.1016/j.colsurfb.2017.11.020 |