Implementing complementary approaches to shape the mechanism of α-synuclein oligomerization as a model of amyloid aggregation
- Autores
- Giampà, Marco; Amundarain, María Julia; Herrera, Maria Georgina; Tonali, Nicolò; Dodero, Veronica Isabel
- Año de publicación
- 2022
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The aggregation of proteins into amyloid fibers is linked to more than forty still incurable cellular and neurodegenerative diseases such as Parkinson’s disease (PD), multiple system atrophy, Alzheimer’s disease and type 2 diabetes, among others. The process of amyloid formation is a main feature of cell degeneration and disease pathogenesis. Despite being methodologically challenging, a complete understanding of the molecular mechanism of aggregation, especially in the early stages, is essential to find new biological targets for innovative therapies. Here, we reviewed selected examples on α-syn showing how complementary approaches, which employ different biophysical techniques and models, can better deal with a comprehensive study of amyloid aggregation. In addition to the monomer aggregation and conformational transition hypothesis, we reported new emerging theories regarding the self-aggregation of α-syn, such as the alpha-helix rich tetramer hypothesis, whose destabilization induce monomer aggregation; and the liquid-liquid phase separation hypothesis, which considers a phase separation of α-syn into liquid droplets as a primary event towards the evolution to aggregates. The final aim of this review is to show how multimodal methodologies provide a complete portrait of α-syn oligomerization and can be successfully extended to other protein aggregation diseases.
Fil: Giampà, Marco. Norwegian University of Science and Technology; Noruega
Fil: Amundarain, María Julia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Física del Sur. Universidad Nacional del Sur. Departamento de Física. Instituto de Física del Sur; Argentina
Fil: Herrera, Maria Georgina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Ruhr Universität Bochum; Alemania
Fil: Tonali, Nicolò. Universite Paris-Saclay;
Fil: Dodero, Veronica Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universitat Bielefeld; Alemania - Materia
-
BIOPHYSICS
MODEL SYSTEMS
OLIGOMER
PROTEIN AGGREGATION
SECONDARY STRUCTURE
Α-SYNUCLEIN - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/203732
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Implementing complementary approaches to shape the mechanism of α-synuclein oligomerization as a model of amyloid aggregationGiampà, MarcoAmundarain, María JuliaHerrera, Maria GeorginaTonali, NicolòDodero, Veronica IsabelBIOPHYSICSMODEL SYSTEMSOLIGOMERPROTEIN AGGREGATIONSECONDARY STRUCTUREΑ-SYNUCLEINhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The aggregation of proteins into amyloid fibers is linked to more than forty still incurable cellular and neurodegenerative diseases such as Parkinson’s disease (PD), multiple system atrophy, Alzheimer’s disease and type 2 diabetes, among others. The process of amyloid formation is a main feature of cell degeneration and disease pathogenesis. Despite being methodologically challenging, a complete understanding of the molecular mechanism of aggregation, especially in the early stages, is essential to find new biological targets for innovative therapies. Here, we reviewed selected examples on α-syn showing how complementary approaches, which employ different biophysical techniques and models, can better deal with a comprehensive study of amyloid aggregation. In addition to the monomer aggregation and conformational transition hypothesis, we reported new emerging theories regarding the self-aggregation of α-syn, such as the alpha-helix rich tetramer hypothesis, whose destabilization induce monomer aggregation; and the liquid-liquid phase separation hypothesis, which considers a phase separation of α-syn into liquid droplets as a primary event towards the evolution to aggregates. The final aim of this review is to show how multimodal methodologies provide a complete portrait of α-syn oligomerization and can be successfully extended to other protein aggregation diseases.Fil: Giampà, Marco. Norwegian University of Science and Technology; NoruegaFil: Amundarain, María Julia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Física del Sur. Universidad Nacional del Sur. Departamento de Física. Instituto de Física del Sur; ArgentinaFil: Herrera, Maria Georgina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Ruhr Universität Bochum; AlemaniaFil: Tonali, Nicolò. Universite Paris-Saclay;Fil: Dodero, Veronica Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universitat Bielefeld; AlemaniaMolecular Diversity Preservation International2022-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/203732Giampà, Marco; Amundarain, María Julia; Herrera, Maria Georgina; Tonali, Nicolò; Dodero, Veronica Isabel; Implementing complementary approaches to shape the mechanism of α-synuclein oligomerization as a model of amyloid aggregation; Molecular Diversity Preservation International; Molecules; 27; 1; 1-2022; 1-211420-3049CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/1420-3049/27/1/88info:eu-repo/semantics/altIdentifier/doi/10.3390/molecules27010088info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:44:24Zoai:ri.conicet.gov.ar:11336/203732instacron: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:34982025-09-03 09:44:24.403CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Implementing complementary approaches to shape the mechanism of α-synuclein oligomerization as a model of amyloid aggregation |
title |
Implementing complementary approaches to shape the mechanism of α-synuclein oligomerization as a model of amyloid aggregation |
spellingShingle |
Implementing complementary approaches to shape the mechanism of α-synuclein oligomerization as a model of amyloid aggregation Giampà, Marco BIOPHYSICS MODEL SYSTEMS OLIGOMER PROTEIN AGGREGATION SECONDARY STRUCTURE Α-SYNUCLEIN |
title_short |
Implementing complementary approaches to shape the mechanism of α-synuclein oligomerization as a model of amyloid aggregation |
title_full |
Implementing complementary approaches to shape the mechanism of α-synuclein oligomerization as a model of amyloid aggregation |
title_fullStr |
Implementing complementary approaches to shape the mechanism of α-synuclein oligomerization as a model of amyloid aggregation |
title_full_unstemmed |
Implementing complementary approaches to shape the mechanism of α-synuclein oligomerization as a model of amyloid aggregation |
title_sort |
Implementing complementary approaches to shape the mechanism of α-synuclein oligomerization as a model of amyloid aggregation |
dc.creator.none.fl_str_mv |
Giampà, Marco Amundarain, María Julia Herrera, Maria Georgina Tonali, Nicolò Dodero, Veronica Isabel |
author |
Giampà, Marco |
author_facet |
Giampà, Marco Amundarain, María Julia Herrera, Maria Georgina Tonali, Nicolò Dodero, Veronica Isabel |
author_role |
author |
author2 |
Amundarain, María Julia Herrera, Maria Georgina Tonali, Nicolò Dodero, Veronica Isabel |
author2_role |
author author author author |
dc.subject.none.fl_str_mv |
BIOPHYSICS MODEL SYSTEMS OLIGOMER PROTEIN AGGREGATION SECONDARY STRUCTURE Α-SYNUCLEIN |
topic |
BIOPHYSICS MODEL SYSTEMS OLIGOMER PROTEIN AGGREGATION SECONDARY STRUCTURE Α-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 aggregation of proteins into amyloid fibers is linked to more than forty still incurable cellular and neurodegenerative diseases such as Parkinson’s disease (PD), multiple system atrophy, Alzheimer’s disease and type 2 diabetes, among others. The process of amyloid formation is a main feature of cell degeneration and disease pathogenesis. Despite being methodologically challenging, a complete understanding of the molecular mechanism of aggregation, especially in the early stages, is essential to find new biological targets for innovative therapies. Here, we reviewed selected examples on α-syn showing how complementary approaches, which employ different biophysical techniques and models, can better deal with a comprehensive study of amyloid aggregation. In addition to the monomer aggregation and conformational transition hypothesis, we reported new emerging theories regarding the self-aggregation of α-syn, such as the alpha-helix rich tetramer hypothesis, whose destabilization induce monomer aggregation; and the liquid-liquid phase separation hypothesis, which considers a phase separation of α-syn into liquid droplets as a primary event towards the evolution to aggregates. The final aim of this review is to show how multimodal methodologies provide a complete portrait of α-syn oligomerization and can be successfully extended to other protein aggregation diseases. Fil: Giampà, Marco. Norwegian University of Science and Technology; Noruega Fil: Amundarain, María Julia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Física del Sur. Universidad Nacional del Sur. Departamento de Física. Instituto de Física del Sur; Argentina Fil: Herrera, Maria Georgina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Ruhr Universität Bochum; Alemania Fil: Tonali, Nicolò. Universite Paris-Saclay; Fil: Dodero, Veronica Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universitat Bielefeld; Alemania |
description |
The aggregation of proteins into amyloid fibers is linked to more than forty still incurable cellular and neurodegenerative diseases such as Parkinson’s disease (PD), multiple system atrophy, Alzheimer’s disease and type 2 diabetes, among others. The process of amyloid formation is a main feature of cell degeneration and disease pathogenesis. Despite being methodologically challenging, a complete understanding of the molecular mechanism of aggregation, especially in the early stages, is essential to find new biological targets for innovative therapies. Here, we reviewed selected examples on α-syn showing how complementary approaches, which employ different biophysical techniques and models, can better deal with a comprehensive study of amyloid aggregation. In addition to the monomer aggregation and conformational transition hypothesis, we reported new emerging theories regarding the self-aggregation of α-syn, such as the alpha-helix rich tetramer hypothesis, whose destabilization induce monomer aggregation; and the liquid-liquid phase separation hypothesis, which considers a phase separation of α-syn into liquid droplets as a primary event towards the evolution to aggregates. The final aim of this review is to show how multimodal methodologies provide a complete portrait of α-syn oligomerization and can be successfully extended to other protein aggregation diseases. |
publishDate |
2022 |
dc.date.none.fl_str_mv |
2022-01 |
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/11336/203732 Giampà, Marco; Amundarain, María Julia; Herrera, Maria Georgina; Tonali, Nicolò; Dodero, Veronica Isabel; Implementing complementary approaches to shape the mechanism of α-synuclein oligomerization as a model of amyloid aggregation; Molecular Diversity Preservation International; Molecules; 27; 1; 1-2022; 1-21 1420-3049 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/203732 |
identifier_str_mv |
Giampà, Marco; Amundarain, María Julia; Herrera, Maria Georgina; Tonali, Nicolò; Dodero, Veronica Isabel; Implementing complementary approaches to shape the mechanism of α-synuclein oligomerization as a model of amyloid aggregation; Molecular Diversity Preservation International; Molecules; 27; 1; 1-2022; 1-21 1420-3049 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.mdpi.com/1420-3049/27/1/88 info:eu-repo/semantics/altIdentifier/doi/10.3390/molecules27010088 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Molecular Diversity Preservation International |
publisher.none.fl_str_mv |
Molecular Diversity Preservation International |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) |
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CONICET Digital (CONICET) |
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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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1842268664099766272 |
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13.13397 |