Broadband terahertz spectroscopy of amino acids

Yi, Wenting; Yu, Jiangping; Xu, Yutian; Wang, Fang; Yu, Qi; Sun, Haijun; Xu, Li; Liu, Yunfei; Jiang, Ling

doi:10.1080/10739149.2016.1270961

Cited by 34 publications

(10 citation statements)

References 42 publications

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“…Kelley [7] studied the absorption spectra of glutamic acid, aspartic acid, glycine, alanine, and seven other amino acids in different modes by using various improved THz spectroscopy detection techniques. Yi et al [8] established a wideband absorption spectrum database of 20 amino acids from 0.1 to 6 THz.…”

Section: Introductionmentioning

confidence: 99%

Terahertz Absorption Properties of Two Solid Amino Acids and Their Aqueous Solutions

Wang

Yang

et al. 2021

International Journal of Optics

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A new type of embedded cyclic olefin copolymer microfluidic chip was designed and combined with terahertz (THz) technology to study the effects of glycine and arginine on the THz wave absorption characteristics. This study aims to understand the interactions between solid amino acid molecules and between amino acid and water molecules and to determine the changes in their microstructure. By observing the intensity of the time domain spectra in the range of 0.2–2.6 THz, we found that, as the concentration of glycine and arginine increased, the THz transmission gradually decreased. It can be inferred that the molecular structure and quantity of different amino acids have different influence on the hydrogen bond, which affects the absorption coefficient in solution. It was also found that the terahertz technique is able to identify the solid amino acid species better, and it can also perform some species identification for liquid amino acids. These results provide a reference for future studies on the terahertz absorption properties of amino acid samples. Moreover, Gaussian16 software was used to calculate the terahertz spectra using the density functional theory, B3LYP functional, and 6-31G basis set. Additionally, Gaussian View6 video software provided the frequency values, molecular vibration modes of the theoretical absorption peaks of glycine, arginine, and its aqueous solutions in the frequency range of 0.2–2.6 THz, which offers theoretical support for future studies.

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Section: Introductionmentioning

confidence: 99%

Terahertz Absorption Properties of Two Solid Amino Acids and Their Aqueous Solutions

Wang

Yang

et al. 2021

International Journal of Optics

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“…Nevertheless, they exhibit differences in the THz absorption spectra: L-val has prominent absorption at 1.11 THz and 4.39 THz; for L-iso, the main absorption peaks were shifted to lower frequencies at 0.85 and 4.27 THz; and finally for L-leu, at 0.66 and 3.68 THz. The authors correlated the differences due to the longer side chains that shift the absorption peaks to lower frequencies [133]. Moreover, the aromatic L-Tyrosine (L-tyr), L-phenylalanine (L-phe) and L-tryptophan (L-try) present a phenyl group on the side chain, and although they have similar structures, the THz spectra are different.…”

Section: Current Status Of Thz Spectroscopy For Protein Researchmentioning

confidence: 99%

“…Table 1. Main THz absorption frequencies observed in the literature [118][119][120][121][122][123][124][125][126][127][128][129][130][131][132][133][134].…”

Section: Current Status Of Thz Spectroscopy For Research On Amino Aci...mentioning

confidence: 99%

“…In Figure 3, the refractive index of these six proteins is reported in the sub-frequency band. Yi et al [133] employed THz-TDS and IR spectroscopy to study all 20 amino acids, accurately collecting their spectra over a wide range from 0.2 to 6 THz (6.67 to 200 cm −1 ). Mixtures in different proportions of amino acids with polyethylene powder, transparent to THz radiation, were made.…”

Section: Current Status Of Thz Spectroscopy For Protein Researchmentioning

confidence: 99%

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Terahertz Spectroscopic Analysis in Protein Dynamics: Current Status

et al. 2022

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Proteins play a key role in living organisms. The study of proteins and their dynamics provides information about their functionality, catalysis and potential alterations towards pathological diseases. Several techniques are used for studying protein dynamics, e.g., magnetic resonance, fluorescence imaging techniques, mid-infrared spectroscopy and biochemical assays. Spectroscopic analysis, based on the use of terahertz (THz) radiation with frequencies between 0.1 and 15 THz (3–500 cm−1), was underestimated by the biochemical community. In recent years, however, the potential of THz spectroscopy in the analysis of both simple structures, such as polypeptide molecules, and complex structures, such as protein complexes, has been demonstrated. The THz absorption spectrum provides some information on proteins: for small molecules the THz spectrum is dominated by individual modes related to the presence of hydrogen bonds. For peptides, the spectral information concerns their secondary structure, while for complex proteins such as globular proteins and viral glycoproteins, spectra also provide information on collective modes. In this short review, we discuss the results obtained by THz spectroscopy in the protein dynamics investigations. In particular, we will illustrate advantages and applications of THz spectroscopy, pointing out the complementary information it may provide.

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“…Considerable amount of data have been accumulated on the THz dielectric spectra of molecular components of cells, such as amino acids, 200 , 201 proteins, 202 – 204 nucleic bases, 205 , 206 and acids, 207 as well as sugars. 32 , 66 At the same time, very limited knowledge about the nonthermal THz-wave effects on such important molecular components of a living cell exist nowadays.…”

Section: Terahertz Exposure Of Biological Objects With Different Levels Of Organizationmentioning

confidence: 99%

Cellular effects of terahertz waves

et al. 2021

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. Significance: An increasing interest in the area of biological effects at exposure of tissues and cells to the terahertz (THz) radiation is driven by a rapid progress in THz biophotonics, observed during the past decades. Despite the attractiveness of THz technology for medical diagnosis and therapy, there is still quite limited knowledge about safe limits of THz exposure. Different modes of THz exposure of tissues and cells, including continuous-wave versus pulsed radiation, various powers, and number and duration of exposure cycles, ought to be systematically studied. Aim: We provide an overview of recent research results in the area of biological effects at exposure of tissues and cells to THz waves. Approach: We start with a brief overview of general features of the THz-wave–tissue interactions, as well as modern THz emitters, with an emphasis on those that are reliable for studying the biological effects of THz waves. Then, we consider three levels of biological system organization, at which the exposure effects are considered: (i) solutions of biological molecules; (ii) cultures of cells, individual cells, and cell structures; and (iii) entire organs or organisms; special attention is devoted to the cellular level. We distinguish thermal and nonthermal mechanisms of THz-wave–cell interactions and discuss a problem of adequate estimation of the THz biological effects’ specificity. The problem of experimental data reproducibility, caused by rareness of the THz experimental setups and an absence of unitary protocols, is also considered. Results: The summarized data demonstrate the current stage of the research activity and knowledge about the THz exposure on living objects. Conclusions: This review helps the biomedical optics community to summarize up-to-date knowledge in the area of cell exposure to THz radiation, and paves the ways for the development of THz safety standards and THz therapeutic applications.

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Broadband terahertz spectroscopy of amino acids

Cited by 34 publications

References 42 publications

Terahertz Absorption Properties of Two Solid Amino Acids and Their Aqueous Solutions

Terahertz Absorption Properties of Two Solid Amino Acids and Their Aqueous Solutions

Terahertz Spectroscopic Analysis in Protein Dynamics: Current Status

Cellular effects of terahertz waves

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