Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy

The morphological features of α-synuclein (AS) amyloid aggregation in vitro and in cells were elucidated at the nanoscale by far-field subdiffraction fluorescence localization microscopy. Labeling AS with rhodamine spiroamide probes allowed us to image AS fibrillar structures by fluorescence stochas...

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Autores principales:	Roberti, Maria Julia, Bossi, Mariano Luis, Jares, Elizabeth Andrea
Publicado:	2012
Materias:	alpha synuclein nanomaterial rhodamine article chemistry color fluorescence microscopy HeLa cell human intracellular space metabolism methodology molecular imaging protein multimerization protein secondary structure alpha-Synuclein Color HeLa Cells Humans Intracellular Space Microscopy, Fluorescence Molecular Imaging Nanostructures Protein Multimerization Protein Structure, Secondary Rhodamines
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00063495_v102_n7_p1598_Roberti http://hdl.handle.net/20.500.12110/paper_00063495_v102_n7_p1598_Roberti
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_00063495_v102_n7_p1598_Roberti
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spelling	paper:paper_00063495_v102_n7_p1598_Roberti2023-06-08T14:31:12Z Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy Roberti, Maria Julia Bossi, Mariano Luis Jares, Elizabeth Andrea alpha synuclein nanomaterial rhodamine article chemistry color fluorescence microscopy HeLa cell human intracellular space metabolism methodology molecular imaging protein multimerization protein secondary structure alpha-Synuclein Color HeLa Cells Humans Intracellular Space Microscopy, Fluorescence Molecular Imaging Nanostructures Protein Multimerization Protein Structure, Secondary Rhodamines The morphological features of α-synuclein (AS) amyloid aggregation in vitro and in cells were elucidated at the nanoscale by far-field subdiffraction fluorescence localization microscopy. Labeling AS with rhodamine spiroamide probes allowed us to image AS fibrillar structures by fluorescence stochastic nanoscopy with an enhanced resolution at least 10-fold higher than that achieved with conventional, diffraction-limited techniques. The implementation of dual-color detection, combined with atomic force microscopy, revealed the propagation of individual fibrils in vitro. In cells, labeled protein appeared as amyloid aggregates of spheroidal morphology and subdiffraction sizes compatible with in vitro supramolecular intermediates perceived independently by atomic force microscopy and cryo-electron tomography. We estimated the number of monomeric protein units present in these minute structures. This approach is ideally suited for the investigation of the molecular mechanisms of amyloid formation both in vitro and in the cellular milieu. © 2012 Biophysical Society. Fil:Roberti, M.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Bossi, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Jares-Erijman, E.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2012 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00063495_v102_n7_p1598_Roberti http://hdl.handle.net/20.500.12110/paper_00063495_v102_n7_p1598_Roberti
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 nanomaterial rhodamine article chemistry color fluorescence microscopy HeLa cell human intracellular space metabolism methodology molecular imaging protein multimerization protein secondary structure alpha-Synuclein Color HeLa Cells Humans Intracellular Space Microscopy, Fluorescence Molecular Imaging Nanostructures Protein Multimerization Protein Structure, Secondary Rhodamines
spellingShingle	alpha synuclein nanomaterial rhodamine article chemistry color fluorescence microscopy HeLa cell human intracellular space metabolism methodology molecular imaging protein multimerization protein secondary structure alpha-Synuclein Color HeLa Cells Humans Intracellular Space Microscopy, Fluorescence Molecular Imaging Nanostructures Protein Multimerization Protein Structure, Secondary Rhodamines Roberti, Maria Julia Bossi, Mariano Luis Jares, Elizabeth Andrea Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy
topic_facet	alpha synuclein nanomaterial rhodamine article chemistry color fluorescence microscopy HeLa cell human intracellular space metabolism methodology molecular imaging protein multimerization protein secondary structure alpha-Synuclein Color HeLa Cells Humans Intracellular Space Microscopy, Fluorescence Molecular Imaging Nanostructures Protein Multimerization Protein Structure, Secondary Rhodamines
description	The morphological features of α-synuclein (AS) amyloid aggregation in vitro and in cells were elucidated at the nanoscale by far-field subdiffraction fluorescence localization microscopy. Labeling AS with rhodamine spiroamide probes allowed us to image AS fibrillar structures by fluorescence stochastic nanoscopy with an enhanced resolution at least 10-fold higher than that achieved with conventional, diffraction-limited techniques. The implementation of dual-color detection, combined with atomic force microscopy, revealed the propagation of individual fibrils in vitro. In cells, labeled protein appeared as amyloid aggregates of spheroidal morphology and subdiffraction sizes compatible with in vitro supramolecular intermediates perceived independently by atomic force microscopy and cryo-electron tomography. We estimated the number of monomeric protein units present in these minute structures. This approach is ideally suited for the investigation of the molecular mechanisms of amyloid formation both in vitro and in the cellular milieu. © 2012 Biophysical Society.
author	Roberti, Maria Julia Bossi, Mariano Luis Jares, Elizabeth Andrea
author_facet	Roberti, Maria Julia Bossi, Mariano Luis Jares, Elizabeth Andrea
author_sort	Roberti, Maria Julia
title	Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy
title_short	Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy
title_full	Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy
title_fullStr	Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy
title_full_unstemmed	Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy
title_sort	imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy
publishDate	2012
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00063495_v102_n7_p1598_Roberti http://hdl.handle.net/20.500.12110/paper_00063495_v102_n7_p1598_Roberti
work_keys_str_mv	AT robertimariajulia imagingnanometersizedasynucleinaggregatesbysuperresolutionfluorescencelocalizationmicroscopy AT bossimarianoluis imagingnanometersizedasynucleinaggregatesbysuperresolutionfluorescencelocalizationmicroscopy AT jareselizabethandrea imagingnanometersizedasynucleinaggregatesbysuperresolutionfluorescencelocalizationmicroscopy
_version_	1768542296256544768

Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy

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