Centre for BioNano Interactions, School of Chemistry and Chemical Biology, University College Dublin , Dublin 4, Ireland.
ACS Nano. 2015 Feb 24;9(2):2157-66. doi: 10.1021/nn506060q. Epub 2015 Feb 12.
The significance of a protein corona on nanoparticles in modulating particle properties and their biological interactions has been widely acknowledged. The protein corona is derived from proteins in biological fluids, many of which are glycosylated. To date, the glycans on the proteins have been largely overlooked in studies of nanoparticle-cell interactions. In this study, we demonstrate that glycosylation of the protein corona plays an important role in maintaining the colloidal stability of nanoparticles and influences nanoparticle-cell interactions. The removal of glycans from the protein corona enhances cell membrane adhesion and cell uptake of nanoparticles in comparison with the fully glycosylated form, resulting in the generation of a pro-inflammatory milieu by macrophages. This study highlights that the post-translational modification of proteins can significantly impact nanoparticle-cell interactions by modulating the protein corona properties.
蛋白质冠在调节纳米颗粒性质及其生物相互作用方面的意义已得到广泛认可。蛋白质冠来源于生物体液中的蛋白质，其中许多是糖基化的。迄今为止，在纳米颗粒-细胞相互作用的研究中，蛋白质上的聚糖在很大程度上被忽视了。在这项研究中，我们证明了蛋白质冠的糖基化在维持纳米颗粒的胶体稳定性和影响纳米颗粒-细胞相互作用方面起着重要作用。与完全糖基化形式相比，从蛋白质冠上去除聚糖可增强纳米颗粒的细胞膜黏附和细胞摄取，导致巨噬细胞产生促炎环境。这项研究强调了蛋白质的翻译后修饰可以通过调节蛋白质冠的性质显著影响纳米颗粒-细胞相互作用。
