Web of Science: 9 cites, Scopus: 9 cites, Google Scholar: cites
Trifluoroethanol Modulates Amyloid Formation by the All α-Helical URN1 FF Domain
Marinelli, Patrizia
Castillo Cano, Virginia (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
Ventura i Zamora, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)

Data: 2013
Resum: 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.
Drets: Aquest 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. Creative Commons
Llengua: Anglès.
Document: article ; recerca ; publishedVersion
Matèria: α-helix ; Amyloid ; FF domain ; Trifluoroethanol ; Molten globule
Publicat a: International Journal of Molecular Sciences, Vol. 14 Núm. 9 (August 2013) , p. 17830-17844, ISSN 1422-0067

DOI: 10.3390/ijms140917830
PMID: 23999589


15 p, 1.8 MB

El registre apareix a les col·leccions:
Articles > Articles de recerca
Articles > Articles publicats

 Registre creat el 2016-11-11, darrera modificació el 2019-02-04



   Favorit i Compartir