Caffeic acid: an antioxidant with novel antisickling properties

It is well documented that caffeic acid (3,4‐dihydroxycinnamic acid) (CA) interacts with and inhibits the oxidative reactions of myoglobin (Mb) and hemoglobin (Hb), and this interaction underlies its antioxidative action in meat. Sickle cell hemoglobin (HbS) is known for its tendency to oxidize more...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Tigist Kassa, James G. Whalin, Mark P. Richards, Abdu I. Alayash
Formato:	article
Lenguaje:	EN
Publicado:	Wiley 2021
Materias:	antioxidants caffeic acid ferryl hemoglobin sickle cell disease Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/9b339d0f101547138ceaf5690cc514db
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:9b339d0f101547138ceaf5690cc514db
record_format	dspace
spelling	oai:doaj.org-article:9b339d0f101547138ceaf5690cc514db2021-12-01T13:36:12ZCaffeic acid: an antioxidant with novel antisickling properties2211-546310.1002/2211-5463.13295https://doaj.org/article/9b339d0f101547138ceaf5690cc514db2021-12-01T00:00:00Zhttps://doi.org/10.1002/2211-5463.13295https://doaj.org/toc/2211-5463It is well documented that caffeic acid (3,4‐dihydroxycinnamic acid) (CA) interacts with and inhibits the oxidative reactions of myoglobin (Mb) and hemoglobin (Hb), and this interaction underlies its antioxidative action in meat. Sickle cell hemoglobin (HbS) is known for its tendency to oxidize more readily than normal HbA in the presence of hydrogen peroxide (H2O2), which leads to a more persistent and highly oxidizing ferryl Hb (HbFe4+). We have investigated the effects of CA on HbS oxidation intermediates, specifically on the ferric/ferryl forms. At a low concentration of H2O2 (0.5‐fold over heme), we observed a fivefold reduction in the amount of HbFe4+ accumulated in a mixture of ferric and H2O2 solution. Higher levels of H2O2 (onefold and twofold over heme) led to a lesser threefold and twofold reduction in the content of HbFe4+, respectively, possibly due to the saturation of the binding sites on the Hb molecule. The most intriguing finding was that when 5‐molar excess CA over heme was used, and a considerable increase in the delay time of HbS polymerization to approximately 200 s was observed. This delay in polymerization of HbS is theoretically sufficient to avoid microcapillary blockage and prevent vasoconstrictions in vivo. Mass spectrometry analysis indicated that CA was more extensively covalently bonded to βCys93 than to βCys112 and αCys104. The dual antioxidant and antisickling properties of CA may be explored further to maximize its therapeutic potential in SCD.Tigist KassaJames G. WhalinMark P. RichardsAbdu I. AlayashWileyarticleantioxidantscaffeic acidferryl hemoglobinsickle cell diseaseBiology (General)QH301-705.5ENFEBS Open Bio, Vol 11, Iss 12, Pp 3293-3303 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	antioxidants caffeic acid ferryl hemoglobin sickle cell disease Biology (General) QH301-705.5
spellingShingle	antioxidants caffeic acid ferryl hemoglobin sickle cell disease Biology (General) QH301-705.5 Tigist Kassa James G. Whalin Mark P. Richards Abdu I. Alayash Caffeic acid: an antioxidant with novel antisickling properties
description	It is well documented that caffeic acid (3,4‐dihydroxycinnamic acid) (CA) interacts with and inhibits the oxidative reactions of myoglobin (Mb) and hemoglobin (Hb), and this interaction underlies its antioxidative action in meat. Sickle cell hemoglobin (HbS) is known for its tendency to oxidize more readily than normal HbA in the presence of hydrogen peroxide (H2O2), which leads to a more persistent and highly oxidizing ferryl Hb (HbFe4+). We have investigated the effects of CA on HbS oxidation intermediates, specifically on the ferric/ferryl forms. At a low concentration of H2O2 (0.5‐fold over heme), we observed a fivefold reduction in the amount of HbFe4+ accumulated in a mixture of ferric and H2O2 solution. Higher levels of H2O2 (onefold and twofold over heme) led to a lesser threefold and twofold reduction in the content of HbFe4+, respectively, possibly due to the saturation of the binding sites on the Hb molecule. The most intriguing finding was that when 5‐molar excess CA over heme was used, and a considerable increase in the delay time of HbS polymerization to approximately 200 s was observed. This delay in polymerization of HbS is theoretically sufficient to avoid microcapillary blockage and prevent vasoconstrictions in vivo. Mass spectrometry analysis indicated that CA was more extensively covalently bonded to βCys93 than to βCys112 and αCys104. The dual antioxidant and antisickling properties of CA may be explored further to maximize its therapeutic potential in SCD.
format	article
author	Tigist Kassa James G. Whalin Mark P. Richards Abdu I. Alayash
author_facet	Tigist Kassa James G. Whalin Mark P. Richards Abdu I. Alayash
author_sort	Tigist Kassa
title	Caffeic acid: an antioxidant with novel antisickling properties
title_short	Caffeic acid: an antioxidant with novel antisickling properties
title_full	Caffeic acid: an antioxidant with novel antisickling properties
title_fullStr	Caffeic acid: an antioxidant with novel antisickling properties
title_full_unstemmed	Caffeic acid: an antioxidant with novel antisickling properties
title_sort	caffeic acid: an antioxidant with novel antisickling properties
publisher	Wiley
publishDate	2021
url	https://doaj.org/article/9b339d0f101547138ceaf5690cc514db
work_keys_str_mv	AT tigistkassa caffeicacidanantioxidantwithnovelantisicklingproperties AT jamesgwhalin caffeicacidanantioxidantwithnovelantisicklingproperties AT markprichards caffeicacidanantioxidantwithnovelantisicklingproperties AT abduialayash caffeicacidanantioxidantwithnovelantisicklingproperties
_version_	1718405130060038144

Caffeic acid: an antioxidant with novel antisickling properties

Ejemplares similares