Photochemistry of tyrosine dimer : When an oxidative lesion of proteins is able to photoinduce further damage

The tyrosine dimer (Tyr2), a covalent bond between two tyrosines (Tyr), is one of the most important modifications of the oxidative damage of proteins. This compound is increasingly used as a marker of aging, stress and pathogenesis. At physiological pH, Tyr2 is able to absorb radiation at wavelengt...

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Autores principales: Reid, Lara Olivia, Vignoni, Mariana, Martins Froment, Nathalie, Thomas, Andrés Héctor, Dántola, María Laura
Formato: Articulo
Lenguaje:Inglés
Publicado: 2019
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Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/141693
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id I19-R120-10915-141693
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Química
Ciencias Exactas
tyrosine dimer
oxidation
photosensitizer
spellingShingle Química
Ciencias Exactas
tyrosine dimer
oxidation
photosensitizer
Reid, Lara Olivia
Vignoni, Mariana
Martins Froment, Nathalie
Thomas, Andrés Héctor
Dántola, María Laura
Photochemistry of tyrosine dimer : When an oxidative lesion of proteins is able to photoinduce further damage
topic_facet Química
Ciencias Exactas
tyrosine dimer
oxidation
photosensitizer
description The tyrosine dimer (Tyr2), a covalent bond between two tyrosines (Tyr), is one of the most important modifications of the oxidative damage of proteins. This compound is increasingly used as a marker of aging, stress and pathogenesis. At physiological pH, Tyr2 is able to absorb radiation at wavelengths significantly present in the solar radiation and artificial sources of light. As a result, when Tyr2 is formed in vivo, a new chromophore appears in the proteins. Despite the biomedical importance of Tyr2, the information of its photochemical properties is limited due to the drawbacks of its synthesis. Therefore, in this work we demonstrate that at physiological pH, Tyr2 undergoes oxidation upon UV excitation yielding different products which conserve the dimeric structure. During its photodegradation different reactive oxygen species, like hydrogen peroxide, superoxide anion and singlet oxygen, are produced. Otherwise, we demonstrated that Tyr2 is able to sensitize the photodegradation of tyrosine. The results presented in this work confirm that Tyr2 can act as a potential photosensitizer, contributing to the harmful effects of UV-A radiation on biological systems.
format Articulo
Articulo
author Reid, Lara Olivia
Vignoni, Mariana
Martins Froment, Nathalie
Thomas, Andrés Héctor
Dántola, María Laura
author_facet Reid, Lara Olivia
Vignoni, Mariana
Martins Froment, Nathalie
Thomas, Andrés Héctor
Dántola, María Laura
author_sort Reid, Lara Olivia
title Photochemistry of tyrosine dimer : When an oxidative lesion of proteins is able to photoinduce further damage
title_short Photochemistry of tyrosine dimer : When an oxidative lesion of proteins is able to photoinduce further damage
title_full Photochemistry of tyrosine dimer : When an oxidative lesion of proteins is able to photoinduce further damage
title_fullStr Photochemistry of tyrosine dimer : When an oxidative lesion of proteins is able to photoinduce further damage
title_full_unstemmed Photochemistry of tyrosine dimer : When an oxidative lesion of proteins is able to photoinduce further damage
title_sort photochemistry of tyrosine dimer : when an oxidative lesion of proteins is able to photoinduce further damage
publishDate 2019
url http://sedici.unlp.edu.ar/handle/10915/141693
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