Implementing complementary approaches to shape the mechanism of α-synuclein oligomerization as a model of amyloid aggregation

dc.creatorGiampà, Marco
dc.creatorAmundarain, María Julia
dc.creatorHerrera, Maria Georgina
dc.creatorTonali, Nicolò
dc.creatorDodero, Veronica Isabel
dc.date2022-01
dc.date.accessioned2023-08-31T00:29:33Z
dc.date.available2023-08-31T00:29:33Z
dc.identifierhttp://hdl.handle.net/11336/203732
dc.identifierGiampà, 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
dc.identifier1420-3049
dc.identifierCONICET Digital
dc.identifierCONICET
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8543480
dc.descriptionThe 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.
dc.descriptionFil: Giampà, Marco. Norwegian University of Science and Technology; Noruega
dc.descriptionFil: 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
dc.descriptionFil: Herrera, Maria Georgina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Ruhr Universität Bochum; Alemania
dc.descriptionFil: Tonali, Nicolò. Universite Paris-Saclay;
dc.descriptionFil: Dodero, Veronica Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universitat Bielefeld; Alemania
dc.formatapplication/pdf
dc.formatapplication/pdf
dc.languageeng
dc.publisherMolecular Diversity Preservation International
dc.relationinfo:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/1420-3049/27/1/88
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/10.3390/molecules27010088
dc.rightsinfo:eu-repo/semantics/openAccess
dc.rightshttps://creativecommons.org/licenses/by/2.5/ar/
dc.subjectBIOPHYSICS
dc.subjectMODEL SYSTEMS
dc.subjectOLIGOMER
dc.subjectPROTEIN AGGREGATION
dc.subjectSECONDARY STRUCTURE
dc.subjectΑ-SYNUCLEIN
dc.subjecthttps://purl.org/becyt/ford/1.6
dc.subjecthttps://purl.org/becyt/ford/1
dc.titleImplementing complementary approaches to shape the mechanism of α-synuclein oligomerization as a model of amyloid aggregation
dc.typeinfo:eu-repo/semantics/article
dc.typeinfo:ar-repo/semantics/artículo
dc.typeinfo:eu-repo/semantics/publishedVersion


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