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

Autores
Roberti, Maria Julia; Fölling, Jonas; Celej, Maria Soledad; Bossi, Mariano Luis; Jovin, Thomas M.; Jares, Elizabeth Andrea
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The morphological features of alpha-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.
Fil: Roberti, Maria Julia. Max Planck Institute For Biophysical Chemistry (karl Friedrich Bonhoeffer Institute); . Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
Fil: Fölling, Jonas. Institut Max Planck Fuer Gesellschaft; Alemania
Fil: Celej, Maria Soledad. Institut Max Planck Fuer Gesellschaft; Alemania
Fil: Bossi, Mariano Luis. Institut Max Planck Fuer Gesellschaft; Alemania
Fil: Jovin, Thomas M.. Institut Max Planck Fuer Gesellschaft; Alemania
Fil: Jares, Elizabeth Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Centro de Investigaciones en Hidratos de Carbono. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigaciones en Hidratos de Carbono; Argentina
Materia
Palm
Nanoscopy
Amyloid
Synuclein
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/72394
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopyRoberti, Maria JuliaFölling, JonasCelej, Maria SoledadBossi, Mariano LuisJovin, Thomas M.Jares, Elizabeth AndreaPalmNanoscopyAmyloidSynucleinhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The morphological features of alpha-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.Fil: Roberti, Maria Julia. Max Planck Institute For Biophysical Chemistry (karl Friedrich Bonhoeffer Institute); . Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; ArgentinaFil: Fölling, Jonas. Institut Max Planck Fuer Gesellschaft; AlemaniaFil: Celej, Maria Soledad. Institut Max Planck Fuer Gesellschaft; AlemaniaFil: Bossi, Mariano Luis. Institut Max Planck Fuer Gesellschaft; AlemaniaFil: Jovin, Thomas M.. Institut Max Planck Fuer Gesellschaft; AlemaniaFil: Jares, Elizabeth Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Centro de Investigaciones en Hidratos de Carbono. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigaciones en Hidratos de Carbono; ArgentinaCell Press2012-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/72394Roberti, Maria Julia; Fölling, Jonas; Celej, Maria Soledad; Bossi, Mariano Luis; Jovin, Thomas M.; et al.; Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy; Cell Press; Biophysical Journal; 102; 7; 4-2012; 1598-16070006-3495CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0006349512002925info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bpj.2012.03.010info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:37:32Zoai:ri.conicet.gov.ar:11336/72394instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:37:32.702CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy
title Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy
spellingShingle Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy
Roberti, Maria Julia
Palm
Nanoscopy
Amyloid
Synuclein
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
dc.creator.none.fl_str_mv Roberti, Maria Julia
Fölling, Jonas
Celej, Maria Soledad
Bossi, Mariano Luis
Jovin, Thomas M.
Jares, Elizabeth Andrea
author Roberti, Maria Julia
author_facet Roberti, Maria Julia
Fölling, Jonas
Celej, Maria Soledad
Bossi, Mariano Luis
Jovin, Thomas M.
Jares, Elizabeth Andrea
author_role author
author2 Fölling, Jonas
Celej, Maria Soledad
Bossi, Mariano Luis
Jovin, Thomas M.
Jares, Elizabeth Andrea
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Palm
Nanoscopy
Amyloid
Synuclein
topic Palm
Nanoscopy
Amyloid
Synuclein
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The morphological features of alpha-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.
Fil: Roberti, Maria Julia. Max Planck Institute For Biophysical Chemistry (karl Friedrich Bonhoeffer Institute); . Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
Fil: Fölling, Jonas. Institut Max Planck Fuer Gesellschaft; Alemania
Fil: Celej, Maria Soledad. Institut Max Planck Fuer Gesellschaft; Alemania
Fil: Bossi, Mariano Luis. Institut Max Planck Fuer Gesellschaft; Alemania
Fil: Jovin, Thomas M.. Institut Max Planck Fuer Gesellschaft; Alemania
Fil: Jares, Elizabeth Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Centro de Investigaciones en Hidratos de Carbono. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigaciones en Hidratos de Carbono; Argentina
description The morphological features of alpha-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.
publishDate 2012
dc.date.none.fl_str_mv 2012-04
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/72394
Roberti, Maria Julia; Fölling, Jonas; Celej, Maria Soledad; Bossi, Mariano Luis; Jovin, Thomas M.; et al.; Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy; Cell Press; Biophysical Journal; 102; 7; 4-2012; 1598-1607
0006-3495
CONICET Digital
CONICET
url http://hdl.handle.net/11336/72394
identifier_str_mv Roberti, Maria Julia; Fölling, Jonas; Celej, Maria Soledad; Bossi, Mariano Luis; Jovin, Thomas M.; et al.; Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy; Cell Press; Biophysical Journal; 102; 7; 4-2012; 1598-1607
0006-3495
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0006349512002925
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bpj.2012.03.010
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Cell Press
publisher.none.fl_str_mv Cell Press
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.069144

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