Cellular Binding of Anionic Nanoparticles is Inhibited by Serum Proteins Independent of Nanoparticle Composition.
Cellular Binding of Anionic Nanoparticles is Inhibited by Serum Proteins Independent of Nanoparticle Composition.
复制标题
DOI：
10.1039/c3bm60121h
复制
发表时间：
2013-09-01
影响因子：
6.6
通讯作者：
Payne CK
中科院分区：
文献类型：
--
作者：
Fleischer CC;Kumar U;Payne CK
用于生物应用的纳米颗粒会遇到细胞外蛋白质的复杂混合物。这些蛋白质在纳米颗粒表面的吸附会形成一个“蛋白质冠”，它可以控制纳米颗粒与细胞环境的相互作用。本研究的目的是确定纳米颗粒的组成和表面修饰如何影响蛋白质-纳米颗粒复合物的细胞结合。我们研究了一组常用的阴离子纳米颗粒的细胞结合：量子点、胶体金纳米颗粒和低密度脂蛋白颗粒，在存在和不存在细胞外蛋白质的情况下。这些实验具有在相同条件下比较不同纳米粒子的优点。结合荧光和暗场显微镜、流式细胞术和光谱学，我们发现这些阴离子纳米颗粒的细胞结合被血清蛋白抑制，而不依赖于纳米颗粒的组成或表面修饰。我们期望这些结果将有助于设计体内应用的纳米颗粒。
Nanoparticles used in biological applications encounter a complex mixture of extracellular proteins. Adsorption of these proteins on the nanoparticle surface results in the formation of a “protein corona,” which can dominate the interaction of the nanoparticle with the cellular environment. The goal of this research was to determine how nanoparticle composition and surface modification affect the cellular binding of protein-nanoparticle complexes. We examined the cellular binding of a collection of commonly used anionic nanoparticles: quantum dots, colloidal gold nanoparticles, and low-density lipoprotein particles, in the presence and absence of extracellular proteins. These experiments have the advantage of comparing different nanoparticles under identical conditions. Using a combination of fluorescence and dark field microscopy, flow cytometry, and spectroscopy, we find that cellular binding of these anionic nanoparticles is inhibited by serum proteins independent of nanoparticle composition or surface modification. We expect these results will aid in the design of nanoparticles for in vivo applications.