Effect of 0.6-THz Continuous-Wave Irradiation on Pathologically Relevant Protein Aggregates

IF 3.9 2区 工程技术 Q2 ENGINEERING, ELECTRICAL & ELECTRONIC
Antonia Intze;Maria Eleonora Temperini;Giorgio Gregori;Federica Verde;Michele Ortolani;Valeria Giliberti
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Abstract

In this article, we investigated the effect of continuous-wave (CW) radiation at 0.6 THz on pathological protein aggregates in the form of amyloid fibrils, i.e., ordered protein complexes linked to neurodegenerative diseases such as Parkinson's and Frontotemporal Dementia. To monitor the effect of terahertz (THz) irradiation, we exploited mid-infrared (mid-IR) vibrational spectroscopy in the amide-I band range, whose lineshape is known to depend on the protein conformation and on how proteins arrange into ordered supramolecular complexes such as fibrils. We coupled the focused THz beam to two different IR-based spectrometers: a conventional Fourier-transform IR (FTIR) Michelson interferometer where the estimated THz electric field is of the order of $\sim$ 1 $\frac{\text{V}}{{{\text {cm}}}}$ ; and an atomic force microscopy-assisted (AFM-IR) near-field spectrometer based on a tunable mid-IR quantum cascade laser, where a much higher electric field ( $\sim$ 0.1 $\frac{{{\text {kV}}}}{\text{cm}}$ ) is mainly achieved thanks to the field enhancement provided by the use of a metallic AFM tip and sample support. In the first case, we interpreted the modification of the amide-I band upon THz irradiation in terms of an increase of the intermolecular forces within fibrils in response to environmental changes induced by THz irradiation (change of hydration). On the other hand, nonthermal effects are observed in the high-THz-field experiments performed on isolated fibril agglomerates in dry condition with the AFM-assisted spectrometer. The IR spectral response upon prolonged THz irradiation contains only the protein contribution and we obtain a different trend compared to the FTIR experiments, i.e., a weakening of the intermolecular forces, here directly induced by THz absorption and not mediated by changes of the environmental conditions. One can envision that further increase of the THz field value, such as with pulsed laser, can lead to the disassembly of protein fibrils.
0.6-THz 连续波辐照对病理相关蛋白质聚集的影响
在本文中,我们研究了 0.6 太赫兹连续波(CW)辐射对淀粉样纤维形式的病理蛋白质聚集体的影响,即与帕金森氏症和额颞叶痴呆症等神经退行性疾病相关的有序蛋白质复合物。为了监测太赫兹(THz)辐照的效果,我们利用了酰胺-I 波段范围的中红外(mid-IIR)振动光谱,已知其线形取决于蛋白质构象以及蛋白质如何排列成有序的超分子复合物(如纤维)。我们将聚焦的太赫兹光束耦合到两种不同的红外光谱仪上:一种是传统的傅立叶变换红外(FTIR)迈克尔逊干涉仪,估计的太赫兹电场为$\sim$1 $\frac{\text{V}}{{\text {cm}}}}$;另一种是基于可调谐中红外量子级联激光器的原子力显微镜辅助(AFM-IR)近场光谱仪,其电场要高得多($\sim$0.1 $\frac{{\text {kV}}}}{\text{cm}}$ ),这主要归功于使用金属 AFM 针尖和样品支撑提供的场增强。在第一种情况下,我们将太赫兹辐照时酰胺-I 波段的变化解释为纤维内部分子间作用力的增加,以响应太赫兹辐照引起的环境变化(水合变化)。另一方面,在使用原子力显微镜辅助光谱仪对干燥条件下的分离纤维团块进行的高太赫兹场实验中,也观察到了非热效应。长时间太赫兹辐照下的红外光谱响应只包含蛋白质的贡献,我们得到了与傅立叶变换红外光谱实验不同的趋势,即分子间作用力减弱,这里是由太赫兹吸收直接引起的,而不是由环境条件的变化介导的。我们可以设想,太赫兹场值的进一步增加(如使用脉冲激光)会导致蛋白质纤维的解体。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
IEEE Transactions on Terahertz Science and Technology
IEEE Transactions on Terahertz Science and Technology ENGINEERING, ELECTRICAL & ELECTRONIC-OPTICS
CiteScore
7.10
自引率
9.40%
发文量
102
期刊介绍: IEEE Transactions on Terahertz Science and Technology focuses on original research on Terahertz theory, techniques, and applications as they relate to components, devices, circuits, and systems involving the generation, transmission, and detection of Terahertz waves.
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