Trifluoroethanol Modulates Amyloid Formation by the All α-Helical URN1 FF Domain

Amyloid fibril formation is implicated in different human diseases. The transition between native α-helices and nonnative intermolecular β-sheets has been suggested to be a trigger of fibrillation in different conformational diseases. The FF domain of the URN1 splicing factor (URN1-FF) is a small al...

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Autores: Marinelli, Patrizia, Castillo Cano, Virginia|||0000-0002-0671-4632, Ventura, Salvador|||0000-0002-9652-6351
Tipo de recurso: artículo
Fecha de publicación:2013
País:España
Institución:Universitat Autònoma de Barcelona
Repositorio:Dipòsit Digital de Documents de la UAB
Idioma:inglés
OAI Identifier:oai:ddd.uab.cat:166715
Acceso en línea:https://ddd.uab.cat/record/166715
https://dx.doi.org/urn:doi:10.3390/ijms140917830
Access Level:acceso abierto
Palabra clave:α-helix
Amyloid
FF domain
Trifluoroethanol
Molten globule
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spelling Trifluoroethanol Modulates Amyloid Formation by the All α-Helical URN1 FF DomainMarinelli, PatriziaCastillo Cano, Virginia|||0000-0002-0671-4632Ventura, Salvador|||0000-0002-9652-6351α-helixAmyloidFF domainTrifluoroethanolMolten globuleAmyloid fibril formation is implicated in different human diseases. The transition between native α-helices and nonnative intermolecular β-sheets has been suggested to be a trigger of fibrillation in different conformational diseases. The FF domain of the URN1 splicing factor (URN1-FF) is a small all-α protein that populates a molten globule (MG) at low pH. Despite the fact that this conformation maintains most of the domain native secondary structure, it progressively converts into β-sheet enriched and highly ordered amyloid fibrils. In this study, we investigated if 2,2,2-trifluoroethanol (TFE) induced conformational changes that affect URN1-FF amyloid formation. Despite TFE having been shown to induce or increase the aggregation of both globular and disordered proteins at moderate concentrations, we demonstrate here that in the case of URN1-FF it reinforces its intrinsic α-helical structure, which competes the formation of aggregated assemblies. In addition, we show that TFE induces conformational diversity in URN1-FF fibrils, in such a way that the fibrils formed in the presence and absence of the cosolvent represent different polymorphs. It is suggested that the effect of TFE on both the soluble and aggregated states of URN1-FF depends on its ability to facilitate hydrogen bonding 22013-01-0120132013-01-01Articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttps://ddd.uab.cat/record/166715https://dx.doi.org/urn:doi:10.3390/ijms140917830reponame:Dipòsit Digital de Documents de la UABinstname:Universitat Autònoma de BarcelonaInglésengopen accesshttp://purl.org/coar/access_right/c_abf2Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, fins i tot amb finalitats comercials, sempre i quan es reconegui l'autoria de l'obra original.https://creativecommons.org/licenses/by/3.0/info:eu-repo/semantics/openAccessoai:ddd.uab.cat:1667152026-06-06T12:50:31Z
dc.title.none.fl_str_mv Trifluoroethanol Modulates Amyloid Formation by the All α-Helical URN1 FF Domain
title Trifluoroethanol Modulates Amyloid Formation by the All α-Helical URN1 FF Domain
spellingShingle Trifluoroethanol Modulates Amyloid Formation by the All α-Helical URN1 FF Domain
Marinelli, Patrizia
α-helix
Amyloid
FF domain
Trifluoroethanol
Molten globule
title_short Trifluoroethanol Modulates Amyloid Formation by the All α-Helical URN1 FF Domain
title_full Trifluoroethanol Modulates Amyloid Formation by the All α-Helical URN1 FF Domain
title_fullStr Trifluoroethanol Modulates Amyloid Formation by the All α-Helical URN1 FF Domain
title_full_unstemmed Trifluoroethanol Modulates Amyloid Formation by the All α-Helical URN1 FF Domain
title_sort Trifluoroethanol Modulates Amyloid Formation by the All α-Helical URN1 FF Domain
dc.creator.none.fl_str_mv Marinelli, Patrizia
Castillo Cano, Virginia|||0000-0002-0671-4632
Ventura, Salvador|||0000-0002-9652-6351
author Marinelli, Patrizia
author_facet Marinelli, Patrizia
Castillo Cano, Virginia|||0000-0002-0671-4632
Ventura, Salvador|||0000-0002-9652-6351
author_role author
author2 Castillo Cano, Virginia|||0000-0002-0671-4632
Ventura, Salvador|||0000-0002-9652-6351
author2_role author
author
dc.subject.none.fl_str_mv α-helix
Amyloid
FF domain
Trifluoroethanol
Molten globule
topic α-helix
Amyloid
FF domain
Trifluoroethanol
Molten globule
description Amyloid fibril formation is implicated in different human diseases. The transition between native α-helices and nonnative intermolecular β-sheets has been suggested to be a trigger of fibrillation in different conformational diseases. The FF domain of the URN1 splicing factor (URN1-FF) is a small all-α protein that populates a molten globule (MG) at low pH. Despite the fact that this conformation maintains most of the domain native secondary structure, it progressively converts into β-sheet enriched and highly ordered amyloid fibrils. In this study, we investigated if 2,2,2-trifluoroethanol (TFE) induced conformational changes that affect URN1-FF amyloid formation. Despite TFE having been shown to induce or increase the aggregation of both globular and disordered proteins at moderate concentrations, we demonstrate here that in the case of URN1-FF it reinforces its intrinsic α-helical structure, which competes the formation of aggregated assemblies. In addition, we show that TFE induces conformational diversity in URN1-FF fibrils, in such a way that the fibrils formed in the presence and absence of the cosolvent represent different polymorphs. It is suggested that the effect of TFE on both the soluble and aggregated states of URN1-FF depends on its ability to facilitate hydrogen bonding
publishDate 2013
dc.date.none.fl_str_mv 2
2013-01-01
2013
2013-01-01
dc.type.none.fl_str_mv Article
http://purl.org/coar/resource_type/c_6501
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://ddd.uab.cat/record/166715
https://dx.doi.org/urn:doi:10.3390/ijms140917830
url https://ddd.uab.cat/record/166715
https://dx.doi.org/urn:doi:10.3390/ijms140917830
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
https://creativecommons.org/licenses/by/3.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
https://creativecommons.org/licenses/by/3.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Dipòsit Digital de Documents de la UAB
instname:Universitat Autònoma de Barcelona
instname_str Universitat Autònoma de Barcelona
reponame_str Dipòsit Digital de Documents de la UAB
collection Dipòsit Digital de Documents de la UAB
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