On the Binding of Congo Red to Amyloid Fibrils

Amyloids are characterized by their capacity to bind Congo red (CR), one of the most used amyloid‐specific dyes. The structural features of CR binding were unknown for years, mainly because of the lack of amyloid structures solved at high resolution. In the last few years, solid‐state NMR spectrosco...

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Autores: Espargaró Colomé, Alba, Llabrés Prat, Salomé, Saupe, Sven J., Curutchet Barat, Carles E., Luque Garriga, F. Xavier, Sabaté Lagunas, Raimon
Tipo de documento: artigo
Estado:Versión aceptada para publicación
Data de publicação:2020
País:España
Recursos:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositório:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:2445/167301
Acesso em linha:https://hdl.handle.net/2445/167301
Access Level:Acceso aberto
Palavra-chave:Amiloïdosi
Polímers
Proteïnes
Prions
Colorants
Amyloidosis
Polymers
Proteins
Coloring matter
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spelling On the Binding of Congo Red to Amyloid FibrilsEspargaró Colomé, AlbaLlabrés Prat, SaloméSaupe, Sven J.Curutchet Barat, Carles E.Luque Garriga, F. XavierSabaté Lagunas, RaimonAmiloïdosiPolímersProteïnesPrionsColorantsAmyloidosisPolymersProteinsPrionsColoring matterAmyloids are characterized by their capacity to bind Congo red (CR), one of the most used amyloid‐specific dyes. The structural features of CR binding were unknown for years, mainly because of the lack of amyloid structures solved at high resolution. In the last few years, solid‐state NMR spectroscopy enabled the determination of the structural features of amyloids, such as the HET‐s prion forming domain (HET‐s PFD), which also has recently been used to determine the amyloid-CR interface at atomic resolution. Herein, we combine spectroscopic data with molecular docking, molecular dynamics, and excitonic quantum/molecular mechanics calculations to examine and rationalize CR binding to amyloids. In contrast to a previous assumption on the binding mode, our results suggest that CR binding to the HET‐s PFD involves a cooperative process entailing the formation of a complex with 1:1 stoichiometry. This provides a molecular basis to explain the bathochromic shift in the maximal absorbance wavelength when CR is bound to amyloids.Wiley-VCH2020202120202020info:eu-repo/semantics/articleinfo:eu-repo/semantics/acceptedVersion4 p.application/pdfhttps://hdl.handle.net/2445/167301Articles publicats en revistes (Farmàcia, Tecnologia Farmacèutica i Fisicoquímica)reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésVersió postprint del document publicat a: https://doi.org/10.1002/anie.201916630Angewandte Chemie-International Edition, 2020, vol. 59, num. 21, p. 8104-8107https://doi.org/10.1002/anie.201916630(c) Wiley-VCH, 2020info:eu-repo/semantics/openAccessoai:recercat.cat:2445/1673012026-05-29T05:05:01Z
dc.title.none.fl_str_mv On the Binding of Congo Red to Amyloid Fibrils
title On the Binding of Congo Red to Amyloid Fibrils
spellingShingle On the Binding of Congo Red to Amyloid Fibrils
Espargaró Colomé, Alba
Amiloïdosi
Polímers
Proteïnes
Prions
Colorants
Amyloidosis
Polymers
Proteins
Prions
Coloring matter
title_short On the Binding of Congo Red to Amyloid Fibrils
title_full On the Binding of Congo Red to Amyloid Fibrils
title_fullStr On the Binding of Congo Red to Amyloid Fibrils
title_full_unstemmed On the Binding of Congo Red to Amyloid Fibrils
title_sort On the Binding of Congo Red to Amyloid Fibrils
dc.creator.none.fl_str_mv Espargaró Colomé, Alba
Llabrés Prat, Salomé
Saupe, Sven J.
Curutchet Barat, Carles E.
Luque Garriga, F. Xavier
Sabaté Lagunas, Raimon
author Espargaró Colomé, Alba
author_facet Espargaró Colomé, Alba
Llabrés Prat, Salomé
Saupe, Sven J.
Curutchet Barat, Carles E.
Luque Garriga, F. Xavier
Sabaté Lagunas, Raimon
author_role author
author2 Llabrés Prat, Salomé
Saupe, Sven J.
Curutchet Barat, Carles E.
Luque Garriga, F. Xavier
Sabaté Lagunas, Raimon
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Amiloïdosi
Polímers
Proteïnes
Prions
Colorants
Amyloidosis
Polymers
Proteins
Prions
Coloring matter
topic Amiloïdosi
Polímers
Proteïnes
Prions
Colorants
Amyloidosis
Polymers
Proteins
Prions
Coloring matter
description Amyloids are characterized by their capacity to bind Congo red (CR), one of the most used amyloid‐specific dyes. The structural features of CR binding were unknown for years, mainly because of the lack of amyloid structures solved at high resolution. In the last few years, solid‐state NMR spectroscopy enabled the determination of the structural features of amyloids, such as the HET‐s prion forming domain (HET‐s PFD), which also has recently been used to determine the amyloid-CR interface at atomic resolution. Herein, we combine spectroscopic data with molecular docking, molecular dynamics, and excitonic quantum/molecular mechanics calculations to examine and rationalize CR binding to amyloids. In contrast to a previous assumption on the binding mode, our results suggest that CR binding to the HET‐s PFD involves a cooperative process entailing the formation of a complex with 1:1 stoichiometry. This provides a molecular basis to explain the bathochromic shift in the maximal absorbance wavelength when CR is bound to amyloids.
publishDate 2020
dc.date.none.fl_str_mv 2020
2020
2020
2021
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/167301
url https://hdl.handle.net/2445/167301
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Versió postprint del document publicat a: https://doi.org/10.1002/anie.201916630
Angewandte Chemie-International Edition, 2020, vol. 59, num. 21, p. 8104-8107
https://doi.org/10.1002/anie.201916630
dc.rights.none.fl_str_mv (c) Wiley-VCH, 2020
info:eu-repo/semantics/openAccess
rights_invalid_str_mv (c) Wiley-VCH, 2020
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 4 p.
application/pdf
dc.publisher.none.fl_str_mv Wiley-VCH
publisher.none.fl_str_mv Wiley-VCH
dc.source.none.fl_str_mv Articles publicats en revistes (Farmàcia, Tecnologia Farmacèutica i Fisicoquímica)
reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15.81155

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