Chiral Plasmonic Fields Probe Structural Order of Biointerfaces.

Chiral Plasmonic Fields Probe Structural Order of Biointerfaces.
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DOI:
10.1021/jacs.8b03634
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发表时间:
2018-07-11
影响因子:
15
通讯作者:
Kadodwala M
Kadodwala M
中科院分区:
化学1区
文献类型:
--
作者:
Kelly C;Tullius R;Lapthorn AJ;Gadegaard N;Cooke G;Barron LD;Karimullah AS;Rotello VM;Kadodwala M

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生物聚合物(如蛋白质)在界面处的结构顺序定义了生物系统与其周围环境的物理和化学相互作用,因此是一系列生物问题中的关键参数。用于常规快速监测生物层中结构顺序的已知光谱方法通常仅应用于具有对取向高度敏感的光谱指纹的模型单组分系统。这种光谱行为不是一般性质,可能需要添加标记。重要的是,这样的技术不能容易地应用于真实的多组分生物层,具有不明确的或未知的组成,并且具有复杂的光谱特征与许多重叠的频带。在这里,我们证明了等离子体场的灵敏度与增强的手性,一个属性被称为超手性,在简单的模型和“真实的”复杂的蛋白质层的全局取向顺序。结构顺序的灵敏度来自超手征场的能力,以检测电偶极-磁偶极响应的层的各向异性的性质,这是通过数值模拟验证。作为模型研究,监测抗体免疫球蛋白G层中随着表面密度增加的取向顺序的演变。作为一个更大的复杂性的例子,超手性领域被证明,没有确切的组成知识,能够监测组成的定性变化如何改变从血清形成的蛋白质层的结构顺序,从而建立作为研究复杂的生物界面的工具的现象的功效。
The structural order of biopolymers, such as proteins, at interfaces defines the physical and chemical interactions of biological systems with their surroundings and is hence a critical parameter in a range of biological problems. Known spectroscopic methods for routine rapid monitoring of structural order in biolayers are generally only applied to model single-component systems that possess a spectral fingerprint which is highly sensitive to orientation. This spectroscopic behavior is not a generic property and may require the addition of a label. Importantly, such techniques cannot readily be applied to real multicomponent biolayers, have ill-defined or unknown compositions, and have complex spectroscopic signatures with many overlapping bands. Here, we demonstrate the sensitivity of plasmonic fields with enhanced chirality, a property referred to as superchirality, to global orientational order within both simple model and “real” complex protein layers. The sensitivity to structural order is derived from the capability of superchiral fields to detect the anisotropic nature of electric dipole–magnetic dipole response of the layer; this is validated by numerical simulations. As a model study, the evolution of orientational order with increasing surface density in layers of the antibody immunoglobulin G was monitored. As an exemplar of greater complexity, superchiral fields are demonstrated, without knowledge of exact composition, to be able to monitor how qualitative changes in composition alter the structural order of protein layers formed from blood serum, thereby establishing the efficacy of the phenomenon as a tool for studying complex biological interfaces.
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