Insights into the molecular mechanism of protein native-like aggregation upon methylglyoxal glycation

Detalhes bibliográficos
Autor(a) principal: Oliveira, Luís M. A.
Data de Publicação: 2013
Outros Autores: Gomes, Ricardo A., Yang, Dennis, Família, Carlos, Lages, Ana, Coelho, Ana V., Murphy, Regina M., Quintas, Alexandre
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10400.26/6831
Resumo: “NOTICE: this is the author’s version of a work that was accepted for publication in Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. Volume 1834, Issue 6, June 2013, Pages 1010–1022, DOI 10.1016/j.bbapap.2012.12.001"
id RCAP_fc7bc5605ce7eeb08ad36981a29a7a97
oai_identifier_str oai:comum.rcaap.pt:10400.26/6831
network_acronym_str RCAP
network_name_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository_id_str 7160
spelling Insights into the molecular mechanism of protein native-like aggregation upon methylglyoxal glycationNative-like aggregationConformational diseasesGlycationMethylglyoxalCytochrome c“NOTICE: this is the author’s version of a work that was accepted for publication in Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. Volume 1834, Issue 6, June 2013, Pages 1010–1022, DOI 10.1016/j.bbapap.2012.12.001""Protein glycation induces structural and stability changes that impair protein function, and is associated with several human neurodegenerative diseases, such as Alzheimer’s disease, Parkinson’s disease and Familial Amyloidotic Polyneuropathy. Recently we have shown that methylglyoxal induces and stabilizes the formation of small native-like aggregates in the amyloidogenic protein insulin and the same was previously shown for α-synuclein. However, the fundamental biophysical mechanism underlying such methylglyoxal-induced protein aggregation is not yet fully understood. In this study, we used the model protein cytochrome c to characterize the specific glycation targets and to investigate the glycation effects on protein structure, stability and aggregation. Methylglyoxal was found modify cytochrome c in a single residue and to induce the formation of cytochrome c native-like aggregates. Additionally, it is shown that methylglyoxal glycation of cytochrome c also results in the formation of a partially unfolded species. Interestingly, the formation of this partially unfolded species is not implicated in the aggregation process, a clear difference from amyloid fibril mechanisms that involve partially or totally unfolded intermediates. Equilibrium-unfolding experiments using guanidinium hydrochloride shows that glycation strongly reduces cytochrome c conformational stability. This reduction is balanced by aggregation that increases conformational stability. The data collected from analytical and spectroscopic techniques along with kinetic analysis based on least-squares parameter fitting and statistical model discrimination permitted the proposal of a comprehensive thermodynamic and kinetic model for native-like aggregation of methylglyoxal glycated cytochrome c."ElsevierRepositório ComumOliveira, Luís M. A.Gomes, Ricardo A.Yang, DennisFamília, CarlosLages, AnaCoelho, Ana V.Murphy, Regina M.Quintas, Alexandre2014-10-20T08:53:42Z2013-06-01T00:00:00Z2013-06-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.26/6831engBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics. Volume 1834, Issue 6, June 2013, Pages 1010–10221570-963910.1016/j.bbapap.2012.12.001info: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:RCAAP2022-10-06T14:51:30Zoai:comum.rcaap.pt:10400.26/6831Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T15:06:05.821081Repositório 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 Insights into the molecular mechanism of protein native-like aggregation upon methylglyoxal glycation
title Insights into the molecular mechanism of protein native-like aggregation upon methylglyoxal glycation
spellingShingle Insights into the molecular mechanism of protein native-like aggregation upon methylglyoxal glycation
Oliveira, Luís M. A.
Native-like aggregation
Conformational diseases
Glycation
Methylglyoxal
Cytochrome c
title_short Insights into the molecular mechanism of protein native-like aggregation upon methylglyoxal glycation
title_full Insights into the molecular mechanism of protein native-like aggregation upon methylglyoxal glycation
title_fullStr Insights into the molecular mechanism of protein native-like aggregation upon methylglyoxal glycation
title_full_unstemmed Insights into the molecular mechanism of protein native-like aggregation upon methylglyoxal glycation
title_sort Insights into the molecular mechanism of protein native-like aggregation upon methylglyoxal glycation
author Oliveira, Luís M. A.
author_facet Oliveira, Luís M. A.
Gomes, Ricardo A.
Yang, Dennis
Família, Carlos
Lages, Ana
Coelho, Ana V.
Murphy, Regina M.
Quintas, Alexandre
author_role author
author2 Gomes, Ricardo A.
Yang, Dennis
Família, Carlos
Lages, Ana
Coelho, Ana V.
Murphy, Regina M.
Quintas, Alexandre
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Repositório Comum
dc.contributor.author.fl_str_mv Oliveira, Luís M. A.
Gomes, Ricardo A.
Yang, Dennis
Família, Carlos
Lages, Ana
Coelho, Ana V.
Murphy, Regina M.
Quintas, Alexandre
dc.subject.por.fl_str_mv Native-like aggregation
Conformational diseases
Glycation
Methylglyoxal
Cytochrome c
topic Native-like aggregation
Conformational diseases
Glycation
Methylglyoxal
Cytochrome c
description “NOTICE: this is the author’s version of a work that was accepted for publication in Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. Volume 1834, Issue 6, June 2013, Pages 1010–1022, DOI 10.1016/j.bbapap.2012.12.001"
publishDate 2013
dc.date.none.fl_str_mv 2013-06-01T00:00:00Z
2013-06-01T00:00:00Z
2014-10-20T08:53:42Z
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/10400.26/6831
url http://hdl.handle.net/10400.26/6831
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. Volume 1834, Issue 6, June 2013, Pages 1010–1022
1570-9639
10.1016/j.bbapap.2012.12.001
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.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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
repository.mail.fl_str_mv
_version_ 1799129931459854336

Registros relacionados