Unravelling the Photoprotection Capacity of Resveratrol on Histidine Oxidation

Autores
Neyra Recky, Jael Rhode; Dántola, María Laura; Lorente, Carolina
Año de publicación
2021
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Exposure to sun radiation causes great oxidative stress and activates a numerous of defense mechanisms in living systems, such as the synthesis of antioxidants. Resveratrol (RSV), a naturally occurring stilbene molecule, has antioxidant properties and is synthesized in large amounts when plants are under high oxidative stress. Likewise, under UV and visible radiation, biomolecules are oxidized, losing their physiological properties and, therefore, avoiding the harmful effects of solar radiation is crucial in order to preserve the functionality of cellular components. In proteins, one essential component that is often susceptible to degradation is the amino acid histidine (His), which can be modified via several oxidizing mechanisms. In this article, we evaluate the photoprotection capacity of RSV in photosensitized oxidation of His, which is initiated with a one-electron transfer reaction, yielding the His radical cation (His•+). The photoprotective properties of RSV are evaluated using kinetics analysis during steady-state irradiation and laser flash photolysis experiments. The experimental results reveal that the presence of RSV in the solution causes an evident decrease of the His consumption initial rates as a result of a reaction between His•+ and RSV that recovers the amino acid. In addition, we conclude that during its antioxidant action, RSV is consumed being a sacrificial antioxidant.
Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas
Materia
Ciencias Exactas
Química
resveratrol
photoprotection
antioxidant
histidine
pterin
photosensitization
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:10915/125436

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network_name_str SEDICI (UNLP)
spelling Unravelling the Photoprotection Capacity of Resveratrol on Histidine OxidationNeyra Recky, Jael RhodeDántola, María LauraLorente, CarolinaCiencias ExactasQuímicaresveratrolphotoprotectionantioxidanthistidinepterinphotosensitizationExposure to sun radiation causes great oxidative stress and activates a numerous of defense mechanisms in living systems, such as the synthesis of antioxidants. Resveratrol (RSV), a naturally occurring stilbene molecule, has antioxidant properties and is synthesized in large amounts when plants are under high oxidative stress. Likewise, under UV and visible radiation, biomolecules are oxidized, losing their physiological properties and, therefore, avoiding the harmful effects of solar radiation is crucial in order to preserve the functionality of cellular components. In proteins, one essential component that is often susceptible to degradation is the amino acid histidine (His), which can be modified via several oxidizing mechanisms. In this article, we evaluate the photoprotection capacity of RSV in photosensitized oxidation of His, which is initiated with a one-electron transfer reaction, yielding the His radical cation (His<sup>•+</sup>). The photoprotective properties of RSV are evaluated using kinetics analysis during steady-state irradiation and laser flash photolysis experiments. The experimental results reveal that the presence of RSV in the solution causes an evident decrease of the His consumption initial rates as a result of a reaction between His<sup>•+</sup> and RSV that recovers the amino acid. In addition, we conclude that during its antioxidant action, RSV is consumed being a sacrificial antioxidant.Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas2021-08-18info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://sedici.unlp.edu.ar/handle/10915/125436enginfo:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2673-7256/1/2/12info:eu-repo/semantics/altIdentifier/issn/2673-7256info:eu-repo/semantics/altIdentifier/doi/10.3390/photochem1020012info: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:UNLP2025-09-03T11:02:08Zoai:sedici.unlp.edu.ar:10915/125436Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-03 11:02:09.077SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Unravelling the Photoprotection Capacity of Resveratrol on Histidine Oxidation
title Unravelling the Photoprotection Capacity of Resveratrol on Histidine Oxidation
spellingShingle Unravelling the Photoprotection Capacity of Resveratrol on Histidine Oxidation
Neyra Recky, Jael Rhode
Ciencias Exactas
Química
resveratrol
photoprotection
antioxidant
histidine
pterin
photosensitization
title_short Unravelling the Photoprotection Capacity of Resveratrol on Histidine Oxidation
title_full Unravelling the Photoprotection Capacity of Resveratrol on Histidine Oxidation
title_fullStr Unravelling the Photoprotection Capacity of Resveratrol on Histidine Oxidation
title_full_unstemmed Unravelling the Photoprotection Capacity of Resveratrol on Histidine Oxidation
title_sort Unravelling the Photoprotection Capacity of Resveratrol on Histidine Oxidation
dc.creator.none.fl_str_mv Neyra Recky, Jael Rhode
Dántola, María Laura
Lorente, Carolina
author Neyra Recky, Jael Rhode
author_facet Neyra Recky, Jael Rhode
Dántola, María Laura
Lorente, Carolina
author_role author
author2 Dántola, María Laura
Lorente, Carolina
author2_role author
author
dc.subject.none.fl_str_mv Ciencias Exactas
Química
resveratrol
photoprotection
antioxidant
histidine
pterin
photosensitization
topic Ciencias Exactas
Química
resveratrol
photoprotection
antioxidant
histidine
pterin
photosensitization
dc.description.none.fl_txt_mv Exposure to sun radiation causes great oxidative stress and activates a numerous of defense mechanisms in living systems, such as the synthesis of antioxidants. Resveratrol (RSV), a naturally occurring stilbene molecule, has antioxidant properties and is synthesized in large amounts when plants are under high oxidative stress. Likewise, under UV and visible radiation, biomolecules are oxidized, losing their physiological properties and, therefore, avoiding the harmful effects of solar radiation is crucial in order to preserve the functionality of cellular components. In proteins, one essential component that is often susceptible to degradation is the amino acid histidine (His), which can be modified via several oxidizing mechanisms. In this article, we evaluate the photoprotection capacity of RSV in photosensitized oxidation of His, which is initiated with a one-electron transfer reaction, yielding the His radical cation (His<sup>•+</sup>). The photoprotective properties of RSV are evaluated using kinetics analysis during steady-state irradiation and laser flash photolysis experiments. The experimental results reveal that the presence of RSV in the solution causes an evident decrease of the His consumption initial rates as a result of a reaction between His<sup>•+</sup> and RSV that recovers the amino acid. In addition, we conclude that during its antioxidant action, RSV is consumed being a sacrificial antioxidant.
Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas
description Exposure to sun radiation causes great oxidative stress and activates a numerous of defense mechanisms in living systems, such as the synthesis of antioxidants. Resveratrol (RSV), a naturally occurring stilbene molecule, has antioxidant properties and is synthesized in large amounts when plants are under high oxidative stress. Likewise, under UV and visible radiation, biomolecules are oxidized, losing their physiological properties and, therefore, avoiding the harmful effects of solar radiation is crucial in order to preserve the functionality of cellular components. In proteins, one essential component that is often susceptible to degradation is the amino acid histidine (His), which can be modified via several oxidizing mechanisms. In this article, we evaluate the photoprotection capacity of RSV in photosensitized oxidation of His, which is initiated with a one-electron transfer reaction, yielding the His radical cation (His<sup>•+</sup>). The photoprotective properties of RSV are evaluated using kinetics analysis during steady-state irradiation and laser flash photolysis experiments. The experimental results reveal that the presence of RSV in the solution causes an evident decrease of the His consumption initial rates as a result of a reaction between His<sup>•+</sup> and RSV that recovers the amino acid. In addition, we conclude that during its antioxidant action, RSV is consumed being a sacrificial antioxidant.
publishDate 2021
dc.date.none.fl_str_mv 2021-08-18
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/10915/125436
url http://sedici.unlp.edu.ar/handle/10915/125436
dc.language.none.fl_str_mv eng
language eng
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info:eu-repo/semantics/altIdentifier/issn/2673-7256
info:eu-repo/semantics/altIdentifier/doi/10.3390/photochem1020012
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)
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instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
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instname_str Universidad Nacional de La Plata
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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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