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利用红外光谱法在等离子体纳米天线上对膜蛋白进行化学固定之后。

Following the Chemical Immobilization of Membrane Proteins on Plasmonic Nanoantennas Using Infrared Spectroscopy.

作者信息

Omeis Fatima, Santos Seica Ana Filipa, Bernard Romain, Javahiraly Nicolas, Majjad Hicham, Moss David, Hellwig Petra

机构信息

Laboratoire de Bioélectrochimie et Spectroscopie, UMR 7140, Université de Strasbourg, CNRS, 4 Rue Blaise Pascal, 67081 Strasbourg, France.

University of Strasbourg Institute for Advanced Studies (USIAS), F-67083 Strasbourg, France.

出版信息

ACS Sens. 2020 Jul 24;5(7):2191-2197. doi: 10.1021/acssensors.0c00824. Epub 2020 Jul 9.

DOI:10.1021/acssensors.0c00824
PMID:32586089
Abstract

Plasmonic nanoantennas are promising sensing platforms for detecting chemical and biological molecules in the infrared region. However, integrating fragile biological molecules such as proteins on plasmonic nanoantennas is an essential requirement in the detection procedure. It is crucial to preserve the structural integrity and functionality of proteins while attaching them. In this study, we attached lactose permease, a large membrane protein, onto plasmonic nanoantennas by means of the nickel-nitrile triacetic acid immobilization technique. We followed the individual steps of the immobilization procedure for different lengths of the nanoantennas. The impact of varying the length of the nanoantennas on the shape of the vibrational signal of the chemical layers and on the protein spectrum was studied. We showed that these large proteins are successfully attached onto the nanoantennas, while the chemical spectra of the immobilization monolayers show a shape deformation which is an effect of the coupling between the vibrational mode and the plasmonic resonance.

摘要

等离子体纳米天线是用于在红外区域检测化学和生物分子的很有前景的传感平台。然而,将诸如蛋白质这样的脆弱生物分子整合到等离子体纳米天线上是检测过程中的一项基本要求。在附着蛋白质时保持其结构完整性和功能至关重要。在本研究中,我们通过镍 - 次氮基三乙酸固定技术将乳糖通透酶(一种大型膜蛋白)附着到等离子体纳米天线上。我们针对不同长度的纳米天线跟踪了固定过程的各个步骤。研究了改变纳米天线长度对化学层振动信号形状以及蛋白质光谱的影响。我们表明这些大型蛋白质成功附着到了纳米天线上,而固定单层的化学光谱显示出形状变形,这是振动模式与等离子体共振之间耦合的结果。

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