Fluorescent N-arylaminonaphthalene sulfonate probes for amyloid aggregation of α-synuclein
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...
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2008
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paper:paper_00063495_v94_n12_p4867_Celej2023-06-08T14:31:18Z Fluorescent N-arylaminonaphthalene sulfonate probes for amyloid aggregation of α-synuclein Jares, Elizabeth Andrea alpha synuclein amyloid arylsulfonic acid derivative fluorescent dye multiprotein complex article chemistry methodology spectrofluorometry alpha-Synuclein Amyloid Arylsulfonates Fluorescent Dyes Multiprotein Complexes Spectrometry, Fluorescence 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. 2008 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00063495_v94_n12_p4867_Celej http://hdl.handle.net/20.500.12110/paper_00063495_v94_n12_p4867_Celej |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (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 Jares, Elizabeth Andrea 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. |
| author |
Jares, Elizabeth Andrea |
| author_facet |
Jares, Elizabeth Andrea |
| author_sort |
Jares, Elizabeth Andrea |
| 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 |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00063495_v94_n12_p4867_Celej http://hdl.handle.net/20.500.12110/paper_00063495_v94_n12_p4867_Celej |
| work_keys_str_mv |
AT jareselizabethandrea fluorescentnarylaminonaphthalenesulfonateprobesforamyloidaggregationofasynuclein |
| _version_ |
1768546001801445376 |