Fluorescent N-arylaminonaphthalene sulfonate probes for amyloid aggregation of α-synuclein

Mostrar todas las versiones(3)

The deposition of fibrillar structures (amyloids) is characteristic of pathological conditions including Alzheimer's and Parkinson's diseases. The detection of protein deposits and the evaluation of their kinetics of aggregation are generally based on fluorescent probes such as thioflavin...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Celej, M.S., Jares-Erijman, E.A., Jovin, T.M.
Formato: Artículo publishedVersion
Publicado: 2008
Materias:
alpha synuclein
amyloid
arylsulfonic acid derivative
fluorescent dye
multiprotein complex
article
chemistry
methodology
spectrofluorometry
alpha-Synuclein
Amyloid
Arylsulfonates
Fluorescent Dyes
Multiprotein Complexes
Spectrometry, Fluorescence
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00063495_v94_n12_p4867_Celej
http://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00063495_v94_n12_p4867_Celej_oai
Aporte de:
Repositorio Digital de la Universidad de Buenos Aires (UBA) de Universidad de Buenos Aires
id I28-R145-paper_00063495_v94_n12_p4867_Celej_oai
record_format dspace
spelling I28-R145-paper_00063495_v94_n12_p4867_Celej_oai2020-10-19 Celej, M.S. Jares-Erijman, E.A. Jovin, T.M. 2008 The deposition of fibrillar structures (amyloids) is characteristic of pathological conditions including Alzheimer's and Parkinson's diseases. The detection of protein deposits and the evaluation of their kinetics of aggregation are generally based on fluorescent probes such as thioflavin T and Congo red. In a search for improved fluorescence tools for studying amyloid formation, we explored the ability of N-arylaminonaphthalene sulfonate (NAS) derivatives to act as noncovalent probes of α-synuclein (AS) fibrillation, a process linked to Parkinson's disease and other neurodegenerative disorders. The compounds bound to fibrillar AS with micromolar Kds, and exhibited fluorescence enhancement, hyperchromism, and high anisotropy. We conclude that the probes experience a hydrophobic environment and/or restricted motion in a polar region. Time- and spectrally resolved emission intensity and anisotropy provided further information regarding structural features of the protein and the dynamics of solvent relaxation. The steady-state and time-resolved parameters changed during the course of aggregation. Compared with thioflavin T, NAS derivatives constitute more sensitive and versatile probes for AS aggregation, and in the case of bis-NAS detect oligomeric as well as fibrillar species. They can function in convenient, continuous assays, thereby providing useful tools for studying the mechanisms of amyloid formation and for high-throughput screening of factors inhibiting and/or reversing protein aggregation in neurodegenerative diseases. © 2008 by the Biophysical Society. Fil:Jares-Erijman, E.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. application/pdf http://hdl.handle.net/20.500.12110/paper_00063495_v94_n12_p4867_Celej info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar Biophys. J. 2008;94(12):4867-4879 alpha synuclein amyloid arylsulfonic acid derivative fluorescent dye multiprotein complex article chemistry methodology spectrofluorometry alpha-Synuclein Amyloid Arylsulfonates Fluorescent Dyes Multiprotein Complexes Spectrometry, Fluorescence Fluorescent N-arylaminonaphthalene sulfonate probes for amyloid aggregation of α-synuclein info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion http://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00063495_v94_n12_p4867_Celej_oai
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-145
collection Repositorio Digital de la Universidad de Buenos Aires (UBA)
topic alpha synuclein
amyloid
arylsulfonic acid derivative
fluorescent dye
multiprotein complex
article
chemistry
methodology
spectrofluorometry
alpha-Synuclein
Amyloid
Arylsulfonates
Fluorescent Dyes
Multiprotein Complexes
Spectrometry, Fluorescence
spellingShingle alpha synuclein
amyloid
arylsulfonic acid derivative
fluorescent dye
multiprotein complex
article
chemistry
methodology
spectrofluorometry
alpha-Synuclein
Amyloid
Arylsulfonates
Fluorescent Dyes
Multiprotein Complexes
Spectrometry, Fluorescence
Celej, M.S.
Jares-Erijman, E.A.
Jovin, T.M.
Fluorescent N-arylaminonaphthalene sulfonate probes for amyloid aggregation of α-synuclein
topic_facet alpha synuclein
amyloid
arylsulfonic acid derivative
fluorescent dye
multiprotein complex
article
chemistry
methodology
spectrofluorometry
alpha-Synuclein
Amyloid
Arylsulfonates
Fluorescent Dyes
Multiprotein Complexes
Spectrometry, Fluorescence
description The deposition of fibrillar structures (amyloids) is characteristic of pathological conditions including Alzheimer's and Parkinson's diseases. The detection of protein deposits and the evaluation of their kinetics of aggregation are generally based on fluorescent probes such as thioflavin T and Congo red. In a search for improved fluorescence tools for studying amyloid formation, we explored the ability of N-arylaminonaphthalene sulfonate (NAS) derivatives to act as noncovalent probes of α-synuclein (AS) fibrillation, a process linked to Parkinson's disease and other neurodegenerative disorders. The compounds bound to fibrillar AS with micromolar Kds, and exhibited fluorescence enhancement, hyperchromism, and high anisotropy. We conclude that the probes experience a hydrophobic environment and/or restricted motion in a polar region. Time- and spectrally resolved emission intensity and anisotropy provided further information regarding structural features of the protein and the dynamics of solvent relaxation. The steady-state and time-resolved parameters changed during the course of aggregation. Compared with thioflavin T, NAS derivatives constitute more sensitive and versatile probes for AS aggregation, and in the case of bis-NAS detect oligomeric as well as fibrillar species. They can function in convenient, continuous assays, thereby providing useful tools for studying the mechanisms of amyloid formation and for high-throughput screening of factors inhibiting and/or reversing protein aggregation in neurodegenerative diseases. © 2008 by the Biophysical Society.
format Artículo
Artículo
publishedVersion
author Celej, M.S.
Jares-Erijman, E.A.
Jovin, T.M.
author_facet Celej, M.S.
Jares-Erijman, E.A.
Jovin, T.M.
author_sort Celej, M.S.
title Fluorescent N-arylaminonaphthalene sulfonate probes for amyloid aggregation of α-synuclein
title_short Fluorescent N-arylaminonaphthalene sulfonate probes for amyloid aggregation of α-synuclein
title_full Fluorescent N-arylaminonaphthalene sulfonate probes for amyloid aggregation of α-synuclein
title_fullStr Fluorescent N-arylaminonaphthalene sulfonate probes for amyloid aggregation of α-synuclein
title_full_unstemmed Fluorescent N-arylaminonaphthalene sulfonate probes for amyloid aggregation of α-synuclein
title_sort fluorescent n-arylaminonaphthalene sulfonate probes for amyloid aggregation of α-synuclein
publishDate 2008
url http://hdl.handle.net/20.500.12110/paper_00063495_v94_n12_p4867_Celej
http://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00063495_v94_n12_p4867_Celej_oai
work_keys_str_mv AT celejms fluorescentnarylaminonaphthalenesulfonateprobesforamyloidaggregationofasynuclein
AT jareserijmanea fluorescentnarylaminonaphthalenesulfonateprobesforamyloidaggregationofasynuclein
AT jovintm fluorescentnarylaminonaphthalenesulfonateprobesforamyloidaggregationofasynuclein
_version_ 1766026512779182080

Ejemplares similares