Probing Specificity of Protein-Protein Interactions with Chiral Plasmonic Nanostructures.

Probing Specificity of Protein-Protein Interactions with Chiral Plasmonic Nanostructures.
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探索蛋白质-蛋白质相互作用与手性等离子体纳米结构的特异性。

DOI:
10.1021/acs.jpclett.9b02288
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发表时间:
2019
期刊:
The journal of physical chemistry letters
影响因子:
--
通讯作者:
M. Kadodwala
M. Kadodwala
中科院分区:
--
文献类型:
--
作者:
Marion Rodier;C. Keijzer;J. Milner;A. Karimullah;L. Barron;N. Gadegaard;A. Lapthorn;M. Kadodwala

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蛋白质-蛋白质相互作用(PPI)在许多生物过程中起着关键作用。因此,区分由特异性相互作用形成的功能重要的明确定义的蛋白质-蛋白质复合物与由非特异性相互作用产生的随机聚集体是一种关键能力。虽然在生物物理工具箱中有许多技术可以快速筛选PPI中的结合亲和力,但没有通用的光谱现象可以快速表征蛋白质-蛋白质复合物的结构。在这项研究中,我们表明,手性等离子体场,由纳米结构的光激发产生的,探测的结构顺序,因此在一个模型抗体-抗原系统的PPI特异性水平。该模型系统的基础是多克隆兔IgG抗体的表面固定化Fab'片段,其在溶液中对牛血清白蛋白(BSA)显示出高特异性。手性等离子体激元场可以区分BSA-Fab'复合物的结构各向异性系综和通过非特异性相互作用形成的随机卵清蛋白(OVA)-Fab'聚集体。该示例性研究证明了手性等离子体场的潜力,其是用于PPI的初始快速高通量筛选的有用蛋白质组学技术的基础。
Protein-protein interactions (PPIs) play a pivotal role in many biological processes. Discriminating functionally important well-defined protein-protein complexes formed by specific interactions from random aggregates produced by non-specific interactions is therefore a critical capability. While there are many techniques in the biophysical tool box which enable rapid screening of binding affinities in PPIs there is no generic spectroscopic phenomenon which provides rapid characterisation of the structure of protein-protein complexes. In this study we show that chiral plasmonic fields, generated by the optical excitation of a nanostructure, probe the structural order and hence level of PPI specificity in a model antibody-antigen system. The basis of the model system is a surface immobilised Fab' fragments of polyclonal rabbit IgG antibodies that displays a high specificity for bovine serum albumin (BSA) in solution. Chiral plasmonic fields can discriminate between the structurally anisotropic ensemble of BSA-Fab' complexes and random ovalbumin (OVA)-Fab' aggregates formed by non-specific interactions. This exemplar study demonstrates the potential of chiral plasmonic fields to be the basis of a useful proteomic technology for the initial rapid high-throughput screening of PPIs.
DOI: 10.1021/jacs.5b04806
发表时间: 2015-07-08
影响因子: 15
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期刊: BIOCHEMISTRY
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发表时间: 2018-02-01
期刊: ACS PHOTONICS
影响因子: 7
作者:
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