The influence of protein adsorption on nanoparticle association with cultured endothelial cells

The influence of protein adsorption on nanoparticle association with cultured endothelial cells
复制标题

DOI:
10.1016/j.biomaterials.2008.09.050
复制
发表时间:
2009-02-01
期刊:
影响因子:
14
通讯作者:
McGrath, James L.
McGrath, James L.
中科院分区:
工程技术1区
文献类型:
--
作者:
Ehrenberg, Morton S.;Friedman, Alan E.;McGrath, James L.

文献摘要

被引文献

相似文献

由于材料的生产规模较小,它们在生物应用(如药物输送、成像或传感应用)中特别有用的特性也使它们具有潜在的危害。已经有相当数量的工作解决了生物流体在材料表面的相互作用,证明了蛋白质对颗粒表面的高亲和力,一些研究了颗粒表面化学在细胞结合中的作用,但是在预期的特定相互作用背景之外的机制研究太少了。在这里,我们使用培养的内皮作为血管运输的模型,我们证明纳米颗粒表面吸附蛋白质的能力表明它们倾向于与细胞结合。对吸附蛋白质的定量分析表明,高结合的纳米颗粒在几秒到几分钟内就能被最大限度地包裹,这表明颗粒表面的蛋白质可以在更长的时间尺度上介导细胞结合。我们还从培养基中去除了许多最丰富的蛋白质,这改变了纳米颗粒上吸附蛋白质的轮廓,但不影响细胞结合的水平。因此,我们得出的结论是,细胞结合不依赖于吸附蛋白的身份,因此不太可能需要与任何特定的细胞受体特异性结合。(C) 2008 Elsevier Ltd版权所有。
As materials are produced at smaller scales, the properties that make them especially useful for biological applications such as drug delivery, imaging or sensing applications also render them potentially harmful. There has been a reasonable amount of work addressing the interactions of biological fluids at material surfaces that demonstrates the high affinity of protein for particle surfaces and some looking at the role of particle surface chemistry in cellular associations, but mechanisms have been too little addressed outside the context of intended, specific interactions. Here, Using Cultured endothelium as a model for vascular transport, we demonstrate that the capacity of nanoparticle surfaces to adsorb protein is indicative of their tendency to associate with cells. Quantification of adsorbed protein shows that high binding nanoparticles are maximally coated in seconds to minutes, indicating that proteins on particle Surfaces can mediate cell association over much longer time scales. We also remove many of the most abundant proteins from culture media which alters the profile of adsorbed proteins on nanoparticles but does not affect the level of cell association. We therefore conclude that cellular association is not dependent on the identity of adsorbed proteins and therefore unlikely to require specific binding to any particular cellular receptors. (C) 2008 Elsevier Ltd. All rights reserved.