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具有可变蛋白质结构和纳米颗粒尺寸的金纳米颗粒上蛋白质吸附的动力学

Kinetics of protein adsorption on gold nanoparticle with variable protein structure and nanoparticle size.

作者信息

Khan S, Gupta A, Verma N C, Nandi C K

机构信息

School of Basic Sciences, Indian Institute of Technology Mandi, Himachal Pradesh 175005, India.

出版信息

J Chem Phys. 2015 Oct 28;143(16):164709. doi: 10.1063/1.4934605.

DOI:10.1063/1.4934605
PMID:26520545
Abstract

The spontaneous protein adsorption on nanomaterial surfaces and the formation of a protein corona around nanoparticles are poorly understood physical phenomena, with high biological relevance. The complexity arises mainly due to the poor knowledge of the structural orientation of the adsorbed proteins onto the nanoparticle surface and difficulties in correlating the protein nanoparticle interaction to the protein corona in real time scale. Here, we provide quantitative insights into the kinetics, number, and binding orientation of a few common blood proteins when they interact with citrate and cetyltriethylammoniumbromide stabilized spherical gold nanoparticles with variable sizes. The kinetics of the protein adsorption was studied experimentally by monitoring the change in hydrodynamic diameter and zeta potential of the nanoparticle-protein complex. To understand the competitive binding of human serum albumin and hemoglobin, time dependent fluorescence quenching was studied using dual fluorophore tags. We have performed molecular docking of three different proteins--human serum albumin, bovine serum albumin, and hemoglobin--on different nanoparticle surfaces to elucidate the possible structural orientation of the adsorbed protein. Our data show that the growth kinetics of a protein corona is exclusively dependent on both protein structure and surface chemistry of the nanoparticles. The study quantitatively suggests that a general physical law of protein adsorption is unlikely to exist as the interaction is unique and specific for a given pair.

摘要

纳米材料表面的自发蛋白质吸附以及纳米颗粒周围蛋白质冠层的形成是目前了解较少但具有高度生物学相关性的物理现象。这种复杂性主要源于对吸附在纳米颗粒表面的蛋白质结构取向了解不足,以及难以在实时尺度上关联蛋白质 - 纳米颗粒相互作用与蛋白质冠层。在此,我们提供了关于几种常见血液蛋白与不同尺寸的柠檬酸盐和十六烷基三乙基溴化铵稳定的球形金纳米颗粒相互作用时的动力学、数量和结合取向的定量见解。通过监测纳米颗粒 - 蛋白质复合物的流体动力学直径和zeta电位的变化,对蛋白质吸附动力学进行了实验研究。为了理解人血清白蛋白和血红蛋白的竞争性结合,使用双荧光团标签研究了时间依赖性荧光猝灭。我们对三种不同的蛋白质——人血清白蛋白、牛血清白蛋白和血红蛋白——在不同的纳米颗粒表面进行了分子对接,以阐明吸附蛋白质的可能结构取向。我们的数据表明,蛋白质冠层的生长动力学完全取决于蛋白质结构和纳米颗粒的表面化学性质。该研究定量表明,由于给定对之间的相互作用是独特且特定的,因此不太可能存在蛋白质吸附的一般物理定律。

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