A quantitative binding study of fibrinogen and human serum albumin to metal oxide nanoparticles by surface plasmon resonance
A quantitative binding study of fibrinogen and human serum albumin to metal oxide nanoparticles by surface plasmon resonance
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DOI：
10.1016/j.bios.2015.05.070
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发表时间：
2015-12-15
影响因子：
12.6
通讯作者：
Gonzalez-Fernandez, Africa
中科院分区：
文献类型：
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作者：
Canoa, Pilar;Simon-Vazquez, Rosana;Gonzalez-Fernandez, Africa
由于金属氧化物纳米颗粒 (NP) 的潜在生物医学应用，血浆蛋白与金属氧化物纳米颗粒 (NP) 的相互作用非常重要。在本研究中，采用新方法定量测量固定在传感器芯片上的 TiO2、CeO2、Al2O3 和 ZnO NP 的纤维蛋白原和人血清白蛋白 (HSA) 的动力学和亲和力。实时表面等离子共振 (SPR) 测量表明，纤维蛋白原与 TiO2 和 CeO2 NP 具有高亲和力（分别为 135 和 40 pM），与 Al2O3 NP 具有中等亲和力（15 nM）相互作用。该数据非常适合描述 1:1 相互作用的 Langmuir 模型。相比之下，HSA 与 TiO2、CeO2 和 Al2O3 NP 的亲和力较低（分别为 80 nM、37 nM 和 21 μM），数据更符合构象变化模型。 TiO2 和CeO2 NPs 与纤维蛋白原的结合速率常数较快(1 x 10(6) M-1 s(-1))，Al2O3 NPs 与纤维蛋白原的结合速率常数较慢(1 x 10(4) M-1 s(-1))。相比之下，HSA 的关联速率常数明显较慢 (1 x 10(3)-1 x 10(4) M-1 s(-1))。蛋白质的结合是可逆的，因此可以快速捕获重复数据。通过使用具有不同化学性质的表面来捕获纳米颗粒（即藻酸盐、NeutrAvidin 和裸金）来评估基质效应的发生。为 NP-蛋白质相互作用确定的亲和力值在很大程度上独立于用于捕获 NP 的底层表面。 (C) 2015 年作者。由 Elsevier B.V. 出版
The interaction of plasma proteins with metal oxide nanoparticles (NPs) is important due to the potential biomedical application of these NPs. In this study, new approaches were applied to measure quantitatively the kinetics and affinities of fibrinogen and human serum albumin (HSA) for TiO2, CeO2, Al2O3 and ZnO NPs immobilized on a sensor chip. Real-time surface plasmon resonance (SPR) measurements showed that fibrinogen interacted with TiO2 and CeO2 NPs with high affinity (135 and 40 pM, respectively) and to Al2O3 NPs with moderate affinity (15 nM). The data fitted well to the Langmuir model describing a 1:1 interaction. In contrast, HSA interacted with TiO2, CeO2 and Al2O3 NPs with lower affinity (80 nM, 37 nM and 21 mu M, respectively) with the data fitting better to the conformational change model. TiO2 and CeO2 NPs had fast association rate constants with fibrinogen (1 x 10(6) M-1 s(-1)) and Al2O3 NPs had a slower association rate constant (1 x 10(4) M-1 s(-1)). By contrast, HSA had markedly slower association rate constants (1 x 10(3)-1 x 10(4) M-1 s(-1)). The binding of the proteins was reversible, thus allowing the rapid capture of data for replicates. The occurrence of matrix effects was evaluated by using surfaces with different chemistries to capture the NPs, namely alginate, NeutrAvidin and bare gold. The affinity values determined for the NP-protein interactions were largely independent of the underlying surface used to capture the NPs. (C) 2015 The Authors. Published by Elsevier B.V.