Characterisation of the protein corona using tunable resistive pulse sensing: determining the change and distribution of a particle's surface charge
Characterisation of the protein corona using tunable resistive pulse sensing: determining the change and distribution of a particle's surface charge
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DOI：
10.1007/s00216-016-9678-6
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发表时间：
2016-08-01
影响因子：
4.3
通讯作者：
Platt, Mark
中科院分区：
文献类型：
--
作者：
Blundell, Emma L. C. J.;Healey, Matthew J.;Platt, Mark
利用可调电阻脉冲传感技术（TRPS）测量了羧基颗粒周围蛋白质电晕的zeta电位。提出了一种用于表征缓冲液、血清和血浆内的zeta电位的简单而快速的测定方法，用于监测颗粒表面上蛋白质的变化、大小和分布。首先，我们测量了溶液中羧基官能化纳米颗粒的zeta电位的变化，该溶液含有生物相关浓度的单个蛋白质，通常在血浆和血清中构成，并观察到室温和37 A ° C测定之间的分布和zeta值的显著差异。该效应是蛋白质依赖性的，并且对于γ-球蛋白，记录了两个温度之间的最大差异，其中对于25和37 A ℃，平均ζ电位分别从-16.7 mV变化至-9.0 mV。该方法还用于监测置于血清和/或血浆中的颗粒。在血清中再次观察到温度依赖性变化，显示在25和37 A ℃下孵育的样品之间的ζ电位差异为4.9 mV;该偏移大于血浆中样品观察到的偏移（0.4 mV）。最后，我们监测了最初置于血清中然后加入5%（V/V）等离子体的颗粒的电晕重定向动力学。提出的技术提供了一个有趣的洞察蛋白质冠结构和动力学的形成在生物相关的解决方案，即高蛋白质，高盐水平，其颗粒的颗粒分析给出了一个测量的颗粒zeta电位的分布，可以提供一个更好地了解纳米粒子在溶液中的行为。
The zeta potential of the protein corona around carboxyl particles has been measured using tunable resistive pulse sensing (TRPS). A simple and rapid assay for characterising zeta potentials within buffer, serum and plasma is presented monitoring the change, magnitude and distribution of proteins on the particle surface. First, we measure the change in zeta potential of carboxyl-functionalised nanoparticles in solutions that contain biologically relevant concentrations of individual proteins, typically constituted in plasma and serum, and observe a significant difference in distributions and zeta values between room temperature and 37 A degrees C assays. The effect is protein dependent, and the largest difference between the two temperatures is recorded for the gamma-globulin protein where the mean zeta potential changes from -16.7 to -9.0 mV for 25 and 37 A degrees C, respectively. This method is further applied to monitor particles placed into serum and/or plasma. A temperature-dependent change is again observed with serum showing a 4.9 mV difference in zeta potential between samples incubated at 25 and 37 A degrees C; this shift was larger than that observed for samples in plasma (0.4 mV). Finally, we monitor the kinetics of the corona reorientation for particles initially placed into serum and then adding 5 % (V/V) plasma. The technology presented offers an interesting insight into protein corona structure and kinetics of formation measured in biologically relevant solutions, i.e. high protein, high salt levels, and its particle-by-particle analysis gives a measure of the distribution of particle zeta potential that may offer a better understanding of the behaviour of nanoparticles in solution.