Federal Institute for Materials Research and Testing (BAM 5.1), Unter den Eichen 87, D-12205 Berlin, Germany.
Colloids Surf B Biointerfaces. 2013 Aug 1;108:110-9. doi: 10.1016/j.colsurfb.2013.02.027. Epub 2013 Mar 4.
The need for a better understanding of nanoparticle-protein interactions and the mechanisms governing the resulting colloidal stability has been emphasised in recent years. In the present contribution, the short and long term colloidal stability of silica nanoparticles (SNPs) and silica-poly(ethylene glycol) nanohybrids (Sil-PEG) have been scrutinised in a protein model system. Well-defined silica nanoparticles are rapidly covered by bovine serum albumin (BSA) and form small clusters after 20min while large agglomerates are detected after 10h depending on both particle size and nanoparticle-protein ratio. Oppositely, Sil-PEG hybrids present suppressive protein adsorption and enhanced short and long term colloidal stability in protein solution. No critical agglomeration was found for either system in the absence of protein, proving that instability found for SNPs must arise as a consequence of protein adsorption and not to high ionic environment. Analysis of the small angle X-ray scattering (SAXS) structure factor indicates a short-range attractive potential between particles in the silica-BSA system, which is in good agreement with a protein bridging agglomeration mechanism. The results presented here point out the importance of the nanoparticle surface properties on the ability to adsorb proteins and how the induced or depressed adsorption may potentially drive the resulting colloidal stability.
近年来,人们越来越需要更好地了解纳米颗粒-蛋白质相互作用以及控制胶体稳定性的机制。在本研究中,我们在蛋白质模型体系中研究了硅胶纳米颗粒(SNP)和硅胶-聚乙二醇纳米杂化体(Sil-PEG)的短期和长期胶体稳定性。粒径和纳米颗粒-蛋白质比例均会影响短时间内(20 分钟)SNP 表面迅速被牛血清白蛋白(BSA)覆盖,形成小的团聚体,长时间后(10 小时)则形成大的团聚体。相反,Sil-PEG 杂化体在蛋白质溶液中具有抑制蛋白质吸附的作用,且具有短期和长期胶体稳定性。在不存在蛋白质的情况下,两种体系都没有发现临界聚集,这证明了 SNPs 的不稳定性是由于蛋白质吸附引起的,而不是由于高离子环境引起的。小角 X 射线散射(SAXS)结构因子分析表明,在硅胶-BSA 体系中颗粒之间存在短程吸引力,这与蛋白质桥接聚集机制非常吻合。本研究结果表明了纳米颗粒表面性质对吸附蛋白质能力的重要性,以及诱导或抑制吸附如何可能潜在地影响胶体稳定性。