分析策略用于检测纳米颗粒-蛋白质相互作用。
Analytical strategies for detecting nanoparticle-protein interactions.
机构信息
School of Chemistry and Chemical Engineering, Shandong University, Jinan, 250100, China.
出版信息
Analyst. 2010 Jul;135(7):1519-30. doi: 10.1039/c0an00075b. Epub 2010 May 26.
Abstract
A significant increase in biomedical applications of nanomaterials and their potential toxicity demands versatile analytical techniques to determine protein-nanoparticle (NP) interactions. These diverse analytical techniques are reviewed. Spectroscopic methods play a significant role in studying binding affinity, binding ratio, and binding mechanisms. To elucidate NP-proteome interactions, chromatography and electrophoresis techniques are applied to separate NP-bound proteins and matrix assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF-MS) to identify these proteins. Since NP-protein binding is a dynamic event, surface plasmon resonance (SPR) and quartz crystal microbalance (QCM) are methods of choice to study the kinetics of NP-protein binding.
摘要
纳米材料在生物医学中的应用显著增加，其潜在毒性也要求有多种分析技术来确定蛋白质-纳米颗粒（NP）的相互作用。本文综述了这些不同的分析技术。光谱方法在研究结合亲和力、结合比和结合机制方面发挥着重要作用。为了阐明 NP-蛋白质组相互作用，应用色谱和电泳技术分离 NP 结合的蛋白质，基质辅助激光解吸电离飞行时间质谱（MALDI-TOF-MS）用于鉴定这些蛋白质。由于 NP-蛋白质的结合是一个动态过程，因此表面等离子体共振（SPR）和石英晶体微天平（QCM）是研究 NP-蛋白质结合动力学的首选方法。
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