Impact of the Nanoparticle-Protein Corona on Colloidal Stability and Protein Structure
Impact of the Nanoparticle-Protein Corona on Colloidal Stability and Protein Structure
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DOI：
10.1021/la301104a
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发表时间：
2012-06-26
期刊：
影响因子：
3.9
通讯作者：
Treuel, Lennart
中科院分区：
文献类型：
--
作者：
Gebauer, Julia S.;Malissek, Marcelina;Treuel, Lennart
在生物流体中，蛋白质可以与纳米颗粒（NP）结合，导致形成所谓的“蛋白质冠”，其在很大程度上限定了颗粒的生物特性。在这里，我们提出了一种新的方法来评估表观结合亲和力的蛋白质的吸附/解吸银纳米粒子的基础上的影响的电晕形成的凝聚动力学的胶体，亲和力来自圆二色性测量补充这些结果，同时阐明吸附的蛋白质的结构变化。用人血清白蛋白作为一个模型，在纳摩尔制度的明显亲和力，导致从这两种方法。总的来说，我们的研究结果现在可以区分NP表面上蛋白质单层和多层的形成。
In biological fluids, proteins may associate with nanoparticles (NPs), leading to the formation of a so-called "protein corona" largely defining the biological identity of the particle. Here, we present a novel approach to assess apparent binding affinities for the adsorption/desorption of proteins to silver NPs based on the impact of the corona formation on the agglomeration kinetics of the colloid, Affinities derived from circular dichroism measurements complement these results, simultaneously elucidating structural changes in the adsorbed protein. Employing human serum albumin as a model, apparent affinities in the nanomolar regime resulted from both approaches. Collectively, our findings now allow discrimination between the formation of protein mono- and multilayers on NP surfaces.