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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/203732
Acceder
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repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling 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 Técnicas2025-09-29T09:34:12Zoai: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:34982025-09-29 09:34:13.071CONICET 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
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
_version_ 1844613057713537024
score 13.069144

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