Protein Adsorption on Hydroxyapatite Nanosensors with Different Crystal Sizes Studied In Situ by a Quartz Crystal Microbalance with the Dissipation Method
Protein Adsorption on Hydroxyapatite Nanosensors with Different Crystal Sizes Studied In Situ by a Quartz Crystal Microbalance with the Dissipation Method
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DOI：
10.1111/j.1551-2916.2009.02957.x
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发表时间：
2009-05-01
影响因子：
3.9
通讯作者：
Tanaka, Junzo
中科院分区：
文献类型：
--
作者：
Ikoma, Toshiyuki;Tagaya, Motohiro;Tanaka, Junzo
采用电泳沉积法在石英晶体微天平的金表面沉积了不同粒径的羟基磷灰石纳米晶。以这种方式形成的纳米传感器用于阐明具有相似pI值的蛋白质的吸附机制。晶体尺寸和a面面积只影响人血清白蛋白的吸附量，而不影响牛血浆纤维蛋白原的吸附量。纳米传感器上的每个吸收层的粘弹性性质，Δ D/Δ f几乎是恒定的。蛋白质吸附机理可以解释如下：白蛋白的游离羧基（负电荷）与钙离子相互作用，纤维蛋白原α C结构域的水合胺基（正电荷）与HAp表面的磷酸根离子相互作用。
Hydroxyapatite (HAp) nanocrystals with different crystal sizes were deposited by the electrophoretic deposition method on the gold surface of a quartz crystal microbalance with a dissipation probe. The nanosensors formed this way were used to elucidate the adsorption mechanism of proteins with a similar pI value. The crystal sizes and the area of the a-plane affected only the adsorption amount of human serum albumin, but not that of bovine plasma fibrinogen. The viscoelastic property, Delta D/Delta f, of each absorbed layer on the nanosensors was almost constant. The protein adsorption mechanism can be explained as follows: the dissociated carboxyl groups (negative charge) of albumin were interacted with calcium ions and the hydrated amine groups (positive charge) at the alpha C domain of fibrinogen were with phosphate ions on the HAp surface.