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Probing the existence of non-thermal Terahertz radiation induced changes of the protein solution structure

During the last decades discussions were taking place on the existence of global, non-thermal structural changes in biological macromolecules induced by Terahertz (THz) radiation. Despite numerous studies, a clear experimental proof of this effect for biological particles in solution is still missin...

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Autores principales: Schroer, Martin A., Schewa, Siawosch, Gruzinov, Andrey Yu., Rönnau, Christian, Lahey-Rudolph, Janine Mia, Blanchet, Clement E., Zickmantel, Till, Song, Young-Hwa, Svergun, Dmitri I., Roessle, Manfred
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8595702/
https://www.ncbi.nlm.nih.gov/pubmed/34785744
http://dx.doi.org/10.1038/s41598-021-01774-6
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author Schroer, Martin A.
Schewa, Siawosch
Gruzinov, Andrey Yu.
Rönnau, Christian
Lahey-Rudolph, Janine Mia
Blanchet, Clement E.
Zickmantel, Till
Song, Young-Hwa
Svergun, Dmitri I.
Roessle, Manfred
author_facet Schroer, Martin A.
Schewa, Siawosch
Gruzinov, Andrey Yu.
Rönnau, Christian
Lahey-Rudolph, Janine Mia
Blanchet, Clement E.
Zickmantel, Till
Song, Young-Hwa
Svergun, Dmitri I.
Roessle, Manfred
author_sort Schroer, Martin A.
collection PubMed
description During the last decades discussions were taking place on the existence of global, non-thermal structural changes in biological macromolecules induced by Terahertz (THz) radiation. Despite numerous studies, a clear experimental proof of this effect for biological particles in solution is still missing. We developed a setup combining THz-irradiation with small angle X-ray scattering (SAXS), which is a sensitive method for detecting the expected structural changes. We investigated in detail protein systems with different shape morphologies (bovine serum albumin, microtubules), which have been proposed to be susceptible to THz-radiation, under variable parameters (THz wavelength, THz power densities up to 6.8 mW/cm(2), protein concentrations). None of the studied systems and conditions revealed structural changes detectable by SAXS suggesting that the expected non-thermal THz-induced effects do not lead to alterations of the overall structures, which are revealed by scattering from dissolved macromolecules. This leaves us with the conclusion that, if such effects are present, these are either local or outside of the spectrum and power range covered by the present study.
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spelling pubmed-85957022021-11-17 Probing the existence of non-thermal Terahertz radiation induced changes of the protein solution structure Schroer, Martin A. Schewa, Siawosch Gruzinov, Andrey Yu. Rönnau, Christian Lahey-Rudolph, Janine Mia Blanchet, Clement E. Zickmantel, Till Song, Young-Hwa Svergun, Dmitri I. Roessle, Manfred Sci Rep Article During the last decades discussions were taking place on the existence of global, non-thermal structural changes in biological macromolecules induced by Terahertz (THz) radiation. Despite numerous studies, a clear experimental proof of this effect for biological particles in solution is still missing. We developed a setup combining THz-irradiation with small angle X-ray scattering (SAXS), which is a sensitive method for detecting the expected structural changes. We investigated in detail protein systems with different shape morphologies (bovine serum albumin, microtubules), which have been proposed to be susceptible to THz-radiation, under variable parameters (THz wavelength, THz power densities up to 6.8 mW/cm(2), protein concentrations). None of the studied systems and conditions revealed structural changes detectable by SAXS suggesting that the expected non-thermal THz-induced effects do not lead to alterations of the overall structures, which are revealed by scattering from dissolved macromolecules. This leaves us with the conclusion that, if such effects are present, these are either local or outside of the spectrum and power range covered by the present study. Nature Publishing Group UK 2021-11-16 /pmc/articles/PMC8595702/ /pubmed/34785744 http://dx.doi.org/10.1038/s41598-021-01774-6 Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Schroer, Martin A.
Schewa, Siawosch
Gruzinov, Andrey Yu.
Rönnau, Christian
Lahey-Rudolph, Janine Mia
Blanchet, Clement E.
Zickmantel, Till
Song, Young-Hwa
Svergun, Dmitri I.
Roessle, Manfred
Probing the existence of non-thermal Terahertz radiation induced changes of the protein solution structure
title Probing the existence of non-thermal Terahertz radiation induced changes of the protein solution structure
title_full Probing the existence of non-thermal Terahertz radiation induced changes of the protein solution structure
title_fullStr Probing the existence of non-thermal Terahertz radiation induced changes of the protein solution structure
title_full_unstemmed Probing the existence of non-thermal Terahertz radiation induced changes of the protein solution structure
title_short Probing the existence of non-thermal Terahertz radiation induced changes of the protein solution structure
title_sort probing the existence of non-thermal terahertz radiation induced changes of the protein solution structure
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8595702/
https://www.ncbi.nlm.nih.gov/pubmed/34785744
http://dx.doi.org/10.1038/s41598-021-01774-6
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