Acrylamide-hemoglobin adduct: A spectroscopic study

Detalhes bibliográficos
Autor(a) principal: Favinha, André G.
Data de Publicação: 2020
Outros Autores: Barreiro, Daniela S., Martins, Joana N., O'Toole, Philip, Pauleta, Sofia R.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10362/133554
Resumo: This work was supported by the Applied Molecular Biosciences Unit – UCIBIO , which is financed by national funds from FCT/MEC ( UIDB/Multi/04378/2020 ).
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spelling Acrylamide-hemoglobin adduct: A spectroscopic studyAcrylamide adductCircular dichroismHemoglobinThermal stabilityVisible spectroscopyAnalytical ChemistryAtomic and Molecular Physics, and OpticsInstrumentationSpectroscopyThis work was supported by the Applied Molecular Biosciences Unit – UCIBIO , which is financed by national funds from FCT/MEC ( UIDB/Multi/04378/2020 ).Acrylamide is a neurotoxic and carcinogenic organic compound that is able to bind to several biomolecules and form adducts, through nucleophilic addition and in vivo by the Maillard Reaction, interfering with the biological functions of these molecules. Hemoglobin is one of the most abundant intracellular blood proteins, and thus it is of high interest to understand whether the binding of acrylamide can alter its properties. The interaction of acrylamide with hemoglobin was assessed in a 20:1 ratio, and after a 72 h-incubation period, a decrease of ca. 50% in the absorbance of the hemoglobin's Soret band was observed at 37 °C. This together with the analysis of circular dichroism spectra indicate that acrylamide binds in close proximity to the heme group. These perturbations were confirmed to not correspond to the loss of the heme group and were mostly reverted after passing the protein through a size-exclusion chromatographic matrix, suggesting a dominant non-covalent interaction for the observed effect. The thermodynamic parameters of unfolding in the absence and presence of acrylamide, suggest an interaction based on H-bonds and van der Waals forces that slightly stabilizes hemoglobin. The oxygen binding capacity of hemoglobin does not seem to be hindered, as no differences in the Q bands were observed in the adduct.DQ - Departamento de QuímicaUCIBIO - Applied Molecular Biosciences UnitRUNFavinha, André G.Barreiro, Daniela S.Martins, Joana N.O'Toole, PhilipPauleta, Sofia R.2023-02-14T01:32:12Z2020-11-052020-11-05T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10362/133554eng1386-1425PURE: 18977493https://doi.org/10.1016/j.saa.2020.118644info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-03-11T05:12:15Zoai:run.unl.pt:10362/133554Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:47:50.284446Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Acrylamide-hemoglobin adduct: A spectroscopic study
title Acrylamide-hemoglobin adduct: A spectroscopic study
spellingShingle Acrylamide-hemoglobin adduct: A spectroscopic study
Favinha, André G.
Acrylamide adduct
Circular dichroism
Hemoglobin
Thermal stability
Visible spectroscopy
Analytical Chemistry
Atomic and Molecular Physics, and Optics
Instrumentation
Spectroscopy
title_short Acrylamide-hemoglobin adduct: A spectroscopic study
title_full Acrylamide-hemoglobin adduct: A spectroscopic study
title_fullStr Acrylamide-hemoglobin adduct: A spectroscopic study
title_full_unstemmed Acrylamide-hemoglobin adduct: A spectroscopic study
title_sort Acrylamide-hemoglobin adduct: A spectroscopic study
author Favinha, André G.
author_facet Favinha, André G.
Barreiro, Daniela S.
Martins, Joana N.
O'Toole, Philip
Pauleta, Sofia R.
author_role author
author2 Barreiro, Daniela S.
Martins, Joana N.
O'Toole, Philip
Pauleta, Sofia R.
author2_role author
author
author
author
dc.contributor.none.fl_str_mv DQ - Departamento de Química
UCIBIO - Applied Molecular Biosciences Unit
RUN
dc.contributor.author.fl_str_mv Favinha, André G.
Barreiro, Daniela S.
Martins, Joana N.
O'Toole, Philip
Pauleta, Sofia R.
dc.subject.por.fl_str_mv Acrylamide adduct
Circular dichroism
Hemoglobin
Thermal stability
Visible spectroscopy
Analytical Chemistry
Atomic and Molecular Physics, and Optics
Instrumentation
Spectroscopy
topic Acrylamide adduct
Circular dichroism
Hemoglobin
Thermal stability
Visible spectroscopy
Analytical Chemistry
Atomic and Molecular Physics, and Optics
Instrumentation
Spectroscopy
description This work was supported by the Applied Molecular Biosciences Unit – UCIBIO , which is financed by national funds from FCT/MEC ( UIDB/Multi/04378/2020 ).
publishDate 2020
dc.date.none.fl_str_mv 2020-11-05
2020-11-05T00:00:00Z
2023-02-14T01:32:12Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10362/133554
url http://hdl.handle.net/10362/133554
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 1386-1425
PURE: 18977493
https://doi.org/10.1016/j.saa.2020.118644
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
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instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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