Infrared Free Electron Laser or Polarized Ultraviolet Photolysis of Hierarchical and Chiral Components of Interleukin-6, AlanylAlanine and Alanine

Interleukin-6 (IL-6) could be decomposed by irradiation of IR-FEL (Infrared free electron laser). Using circularly polarized and other UV light and IR-FEL light, photolysis of hierarchical components of cast films of IL-6, namely deuterated aqueous solutions of enantiomers of dipeptide (L-alanyl-L-a...

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Main Authors: Nanami Fujisawa, Yuika Onami, Takayasu Kawasaki, Tomoyuki Haraguchi, Takashiro Akitsu, Koichi Tsukiyama
Format: Article
Language:English
Published: Shahid Beheshti University of Medical Sciences 2021-01-01
Series:Trends in Peptide and Protein Sciences
Subjects:
Online Access:https://journals.sbmu.ac.ir/protein/article/view/33129
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author Nanami Fujisawa
Yuika Onami
Takayasu Kawasaki
Tomoyuki Haraguchi
Takashiro Akitsu
Koichi Tsukiyama
author_facet Nanami Fujisawa
Yuika Onami
Takayasu Kawasaki
Tomoyuki Haraguchi
Takashiro Akitsu
Koichi Tsukiyama
author_sort Nanami Fujisawa
collection DOAJ
description Interleukin-6 (IL-6) could be decomposed by irradiation of IR-FEL (Infrared free electron laser). Using circularly polarized and other UV light and IR-FEL light, photolysis of hierarchical components of cast films of IL-6, namely deuterated aqueous solutions of enantiomers of dipeptide (L-alanyl-L-alanine (Ala-ala) or D-alanyl-D-alanine) and enantiomers of amino acid (L-alanine (Ala) or D-alanine) was investigated whether specific bonds can be broken by absorption of light (not due to heat). In addition, IR-FEL irradiation to powder as well as crystal structure determination for L-Ala and D-Ala at 173 and 293 K were also carried out to confirm reproducibility in the solid state about long-lasting controversy about Salam’ hypothesis associated with chirality exhibiting structural phase transition at different temperature. Subunits of IL-6 (dipeptide and amino acid) could not be decomposed by polarized IR-FEL nor UV (ultraviolet) light regardless of their chirality. All experimental methods tested in this study failed to prove Salam's hypothesis, positively. Consequently, secondary structure of IL-6 was found to be easier to be damaged by IR-FEL than covalent bonds. HIGHLIGHTS • Interleukin 6 (IL-6) was decomposed by irradiation of IR-FEL (Infrared free electron laser). • Parts of IL-6 (dipeptide and amino acid) was not decomposed by polarized IR-FEL nor UV (ultraviolet) light regardless of their chirality. • Secondary structure of IL-6 was easier to be damaged by IR-FEL than covalent bonds.
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spelling doaj.art-f7898cc6871a4f66b03a3784898f3a942022-12-21T17:17:16ZengShahid Beheshti University of Medical SciencesTrends in Peptide and Protein Sciences2538-24462021-01-015111 (e8)10.22037/tpps.v5i.3312933129Infrared Free Electron Laser or Polarized Ultraviolet Photolysis of Hierarchical and Chiral Components of Interleukin-6, AlanylAlanine and AlanineNanami FujisawaYuika OnamiTakayasu KawasakiTomoyuki HaraguchiTakashiro AkitsuKoichi TsukiyamaInterleukin-6 (IL-6) could be decomposed by irradiation of IR-FEL (Infrared free electron laser). Using circularly polarized and other UV light and IR-FEL light, photolysis of hierarchical components of cast films of IL-6, namely deuterated aqueous solutions of enantiomers of dipeptide (L-alanyl-L-alanine (Ala-ala) or D-alanyl-D-alanine) and enantiomers of amino acid (L-alanine (Ala) or D-alanine) was investigated whether specific bonds can be broken by absorption of light (not due to heat). In addition, IR-FEL irradiation to powder as well as crystal structure determination for L-Ala and D-Ala at 173 and 293 K were also carried out to confirm reproducibility in the solid state about long-lasting controversy about Salam’ hypothesis associated with chirality exhibiting structural phase transition at different temperature. Subunits of IL-6 (dipeptide and amino acid) could not be decomposed by polarized IR-FEL nor UV (ultraviolet) light regardless of their chirality. All experimental methods tested in this study failed to prove Salam's hypothesis, positively. Consequently, secondary structure of IL-6 was found to be easier to be damaged by IR-FEL than covalent bonds. HIGHLIGHTS • Interleukin 6 (IL-6) was decomposed by irradiation of IR-FEL (Infrared free electron laser). • Parts of IL-6 (dipeptide and amino acid) was not decomposed by polarized IR-FEL nor UV (ultraviolet) light regardless of their chirality. • Secondary structure of IL-6 was easier to be damaged by IR-FEL than covalent bonds.https://journals.sbmu.ac.ir/protein/article/view/33129interleukin 6alanyl-alaninealanineir-felpolarized lightsalam hypothesis
spellingShingle Nanami Fujisawa
Yuika Onami
Takayasu Kawasaki
Tomoyuki Haraguchi
Takashiro Akitsu
Koichi Tsukiyama
Infrared Free Electron Laser or Polarized Ultraviolet Photolysis of Hierarchical and Chiral Components of Interleukin-6, AlanylAlanine and Alanine
Trends in Peptide and Protein Sciences
interleukin 6
alanyl-alanine
alanine
ir-fel
polarized light
salam hypothesis
title Infrared Free Electron Laser or Polarized Ultraviolet Photolysis of Hierarchical and Chiral Components of Interleukin-6, AlanylAlanine and Alanine
title_full Infrared Free Electron Laser or Polarized Ultraviolet Photolysis of Hierarchical and Chiral Components of Interleukin-6, AlanylAlanine and Alanine
title_fullStr Infrared Free Electron Laser or Polarized Ultraviolet Photolysis of Hierarchical and Chiral Components of Interleukin-6, AlanylAlanine and Alanine
title_full_unstemmed Infrared Free Electron Laser or Polarized Ultraviolet Photolysis of Hierarchical and Chiral Components of Interleukin-6, AlanylAlanine and Alanine
title_short Infrared Free Electron Laser or Polarized Ultraviolet Photolysis of Hierarchical and Chiral Components of Interleukin-6, AlanylAlanine and Alanine
title_sort infrared free electron laser or polarized ultraviolet photolysis of hierarchical and chiral components of interleukin 6 alanylalanine and alanine
topic interleukin 6
alanyl-alanine
alanine
ir-fel
polarized light
salam hypothesis
url https://journals.sbmu.ac.ir/protein/article/view/33129
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