ARC Centre of Excellence for Functional Nanomaterials, School of Chemical Engineering, University of New South Wales, Sydney NSW 2052, Australia.
Langmuir. 2011 Jan 18;27(2):843-50. doi: 10.1021/la104278m. Epub 2010 Dec 20.
A facile method of stabilizing magnetic iron oxide nanoparticles (MNPs) in biological media (RPMI-1640) via surface modification with fetal bovine serum (FBS) is presented herein. Dynamic light scattering (DLS) shows that the size of the MNP aggregates can be maintained at 190 ± 2 nm for up to 16 h in an RPMI 1640 culture medium containing ≥4 vol % FBS. Under transmission electron microscopy (TEM), a layer of protein coating is observed to cover the MNP surface following treatment with FBS. The adsorption of proteins is further confirmed by X-ray photoelectron spectroscopy (XPS). Gel electrophoresis and LC-MS/MS studies reveal that complement factor H, antithrombin, complement factor I, α-1-antiproteinase, and apolipoprotein E are the proteins most strongly attached to the surface of an MNP. These surface-adsorbed proteins serve as a linker that aids the adsorption of other serum proteins, such as albumin, which otherwise adsorb poorly onto MNPs. The size stability of FBS-treated MNPs in biological media is attributed to the secondary adsorbed proteins, and the size stability in biological media can be maintained only when both the surface-adsorbed proteins and the secondary adsorbed proteins are present on the particle's surface.
本文提出了一种通过胎牛血清(FBS)表面修饰在生物介质(RPMI-1640)中稳定磁性氧化铁纳米颗粒(MNPs)的简便方法。动态光散射(DLS)表明,在含有≥4 体积% FBS 的 RPMI 1640 培养基中,MNP 聚集体的尺寸可在 16 小时内保持在 190±2nm。在透射电子显微镜(TEM)下,观察到在 FBS 处理后,在 MNP 表面覆盖有一层蛋白质涂层。通过 X 射线光电子能谱(XPS)进一步证实了蛋白质的吸附。凝胶电泳和 LC-MS/MS 研究表明,补体因子 H、抗凝血酶、补体因子 I、α-1-抗蛋白酶和载脂蛋白 E 是与 MNP 表面结合最强的蛋白质。这些表面吸附的蛋白质作为一种连接物,有助于其他血清蛋白(如白蛋白)的吸附,否则白蛋白在 MNPs 上吸附不良。FBS 处理的 MNPs 在生物介质中的尺寸稳定性归因于次级吸附的蛋白质,并且只有当表面吸附的蛋白质和次级吸附的蛋白质都存在于颗粒表面时,才能维持在生物介质中的尺寸稳定性。