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

Autores
Reid, Lara Olivia; Vignoni, Mariana; Martins Froment, Nathalie; Thomas, Andrés Héctor; Dántola, María Laura
Año de publicación
2019
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas
Materia
Química
Ciencias Exactas
tyrosine dimer
oxidation
photosensitizer
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/141693
Acceder
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oai_identifier_str oai:sedici.unlp.edu.ar:10915/141693
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Photochemistry of tyrosine dimer : When an oxidative lesion of proteins is able to photoinduce further damageReid, Lara OliviaVignoni, MarianaMartins Froment, NathalieThomas, Andrés HéctorDántola, María LauraQuímicaCiencias Exactastyrosine dimeroxidationphotosensitizerThe 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.Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas2019-07-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf1732-1741http://sedici.unlp.edu.ar/handle/10915/141693enginfo:eu-repo/semantics/altIdentifier/issn/1474-9092info:eu-repo/semantics/altIdentifier/issn/1474-905xinfo:eu-repo/semantics/altIdentifier/doi/10.1039/c9pp00182dinfo:eu-repo/semantics/altIdentifier/pmid/31070216info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:32:11Zoai:sedici.unlp.edu.ar:10915/141693Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:32:12.216SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Photochemistry of tyrosine dimer : When an oxidative lesion of proteins is able to photoinduce further damage
title Photochemistry of tyrosine dimer : When an oxidative lesion of proteins is able to photoinduce further damage
spellingShingle Photochemistry of tyrosine dimer : When an oxidative lesion of proteins is able to photoinduce further damage
Reid, Lara Olivia
Química
Ciencias Exactas
tyrosine dimer
oxidation
photosensitizer
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
dc.creator.none.fl_str_mv Reid, Lara Olivia
Vignoni, Mariana
Martins Froment, Nathalie
Thomas, Andrés Héctor
Dántola, María Laura
author Reid, Lara Olivia
author_facet Reid, Lara Olivia
Vignoni, Mariana
Martins Froment, Nathalie
Thomas, Andrés Héctor
Dántola, María Laura
author_role author
author2 Vignoni, Mariana
Martins Froment, Nathalie
Thomas, Andrés Héctor
Dántola, María Laura
author2_role author
author
author
author
dc.subject.none.fl_str_mv Química
Ciencias Exactas
tyrosine dimer
oxidation
photosensitizer
topic Química
Ciencias Exactas
tyrosine dimer
oxidation
photosensitizer
dc.description.none.fl_txt_mv 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.
Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas
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.
publishDate 2019
dc.date.none.fl_str_mv 2019-07-10
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/141693
url http://sedici.unlp.edu.ar/handle/10915/141693
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/1474-9092
info:eu-repo/semantics/altIdentifier/issn/1474-905x
info:eu-repo/semantics/altIdentifier/doi/10.1039/c9pp00182d
info:eu-repo/semantics/altIdentifier/pmid/31070216
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.format.none.fl_str_mv application/pdf
1732-1741
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 13.070432

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