Reusable hydroxyapatite nanocrystal sensors for protein adsorption
Reusable hydroxyapatite nanocrystal sensors for protein adsorption
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DOI：
10.1088/1468-6996/11/4/045002
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发表时间：
2010-02
影响因子：
5.5
通讯作者：
M. Tagaya;T. Ikoma;N. Hanagata;D. Chakarov;B. Kasemo;J. Tanaka
中科院分区：
文献类型：
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作者：
M. Tagaya;T. Ikoma;N. Hanagata;D. Chakarov;B. Kasemo;J. Tanaka
摘要采用傅里叶变换红外光谱（FTIR）和石英晶体微天平（QCM-D）监测技术，研究了纤维蛋白原和胎牛血清在羟基磷灰石（HAp）生物传感器上吸附和去除的重复性。通过电泳沉积将HAp纳米晶体涂覆在金涂覆的石英传感器上。通过（i）氨/过氧化氢混合物（APM）、（ii）紫外光（UV）、（iii）UV/APM、（iv）APM/UV和（v）十二烷基硫酸钠（SDS）处理来去除吸附在HAp传感器上的蛋白质。红外光谱的重复使用的表面显示，APM和SDS处理留下的肽片段或蛋白质吸附在表面上，而其他方法成功地去除蛋白质。QCM-D测量表明，在去除处理中，纤维蛋白原缓慢吸附在第一个周期，因为接触角测量揭示的表面润湿性的变化。SDS处理在去除蛋白质方面无效。APM或UV处理降低了重复使用的HAp传感器的频移。UV/APM处理没有引起频率偏移，但降低了耗散偏移。因此，我们得出结论，APM/UV处理是最有用的方法，用于再现蛋白质吸附行为的HAp传感器。
Abstract The repeatability of the adsorption and removal of fibrinogen and fetal bovine serum on hydroxyapatite (HAp) nanocrystal sensors was investigated by Fourier transform infrared (FTIR) spectroscopy and quartz crystal microbalance with dissipation (QCM-D) monitoring technique. The HAp nanocrystals were coated on a gold-coated quartz sensor by electrophoretic deposition. Proteins adsorbed on the HAp sensors were removed by (i) ammonia/hydrogen peroxide mixture (APM), (ii) ultraviolet light (UV), (iii) UV/APM, (iv) APM/UV and (v) sodium dodecyl sulfate (SDS) treatments. FTIR spectra of the reused surfaces revealed that the APM and SDS treatments left peptide fragments or the proteins adsorbed on the surfaces, whereas the other methods successfully removed the proteins. The QCM-D measurements indicated that in the removal treatments, fibrinogen was slowly adsorbed in the first cycle because of the change in surface wettability revealed by contact angle measurements. The SDS treatment was not effective in removing proteins. The APM or UV treatment decreased the frequency shifts for the reused HAp sensors. The UV/APM treatment did not induce the frequency shifts but decreased the dissipation shifts. Therefore, we conclude that the APM/UV treatment is the most useful method for reproducing protein adsorption behavior on HAp sensors.