Protein corona changes mediated by surface modification of amorphous silica nanoparticles suppress acute toxicity and activation of intrinsic coagulation cascade in mice
Protein corona changes mediated by surface modification of amorphous silica nanoparticles suppress acute toxicity and activation of intrinsic coagulation cascade in mice
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DOI：
10.1088/0957-4484/26/24/245101
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发表时间：
2015-06
期刊：
影响因子：
3.5
通讯作者：
Tokuyuki Yoshida;Y. Yoshioka;Y. Morishita;Michihiko Aoyama;S. Tochigi;T. Hirai;Kota Tanaka;K. Nagano
中科院分区：
文献类型：
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作者：
Tokuyuki Yoshida;Y. Yoshioka;Y. Morishita;Michihiko Aoyama;S. Tochigi;T. Hirai;Kota Tanaka;K. Nagano
最近，纳米材料介导的生物效应已被证明是由纳米材料与生物流体中的某些种类的蛋白质的相互作用所控制的，并且纳米材料的物理特性决定了它们与蛋白质相互作用的程度和类型。在这里，我们研究了直径为70 nm（nSP 70）的无定形二氧化硅纳米粒子的表面性质，它们与生物液体中的一些蛋白质的相互作用，以及它们在小鼠静脉给药后的毒性之间的关系。用氨基（nSP 70-N）对nSP 70进行表面改性防止了在nSP 70处理组小鼠中发现的急性致死性和凝血级联的异常激活。由于我们以前的研究表明，凝血因子XII在nSP 70介导的凝血级联反应的异常激活中发挥作用，我们研究了nSP 70和nSP 70-N与凝血因子XII的相互作用。与nSP 70-N相比，凝血因子XII与nSP 70表面的结合程度更大，因此，与nSP 70-N相比，观察到nSP 70对凝血因子XII的活化程度更高。总的来说，我们的研究结果表明，通过改变表面性质来控制nSP 70与凝血因子XII的相互作用将有助于抑制nSP 70介导的凝血级联反应的异常激活。
Recently, nanomaterial-mediated biological effects have been shown to be governed by the interaction of nanomaterials with some kinds of proteins in biological fluids, and the physical characteristics of the nanomaterials determine the extent and type of their interactions with proteins. Here, we examined the relationships between the surface properties of amorphous silica nanoparticles with diameters of 70 nm (nSP70), their interactions with some proteins in biological fluids, and their toxicity in mice after intravenous administration. The surface modification of nSP70 with amino groups (nSP70-N) prevented acute lethality and abnormal activation of the coagulation cascade found in the nSP70-treated group of mice. Since our previous study showed that coagulation factor XII played a role in the nSP70-mediated abnormal activation of the coagulation cascade, we examined the interaction of nSP70 and nSP70-N with coagulation factor XII. Coagulation factor XII bonded to the surface of nSP70 to a greater extent than that observed for nSP70-N, and consequently more activation of coagulation factor XII was observed for nSP70 than for nSP70-N. Collectively, our results suggest that controlling the interaction of nSP70 with blood coagulation factor XII by modifying the surface properties would help to inhibit the nSP70-mediated abnormal activation of the blood coagulation cascade.