Recent High-Resolution Structures of Amyloids Involved in Neurodegenerative Diseases

Amyloids are highly ordered aggregates composed of proteins or peptides. They are involved in several pathologies, including hallmark neurodegenerative disorders such as Alzheimer’s (AD) and Parkinson’s (PD). Individuals affected by these diseases accumulate in their brains amyloids inclusions compo...

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Autor principal:	Rodrigo Diaz-Espinoza
Formato:	article
Lenguaje:	EN
Publicado:	Frontiers Media S.A. 2021
Materias:	neurodegenerative diseases misfolding amyloid structure Aβ Tau Neurosciences. Biological psychiatry. Neuropsychiatry RC321-571
Acceso en línea:	https://doaj.org/article/68da2e7d55264739ae58b2ab53218f2e
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spelling	oai:doaj.org-article:68da2e7d55264739ae58b2ab53218f2e2021-11-19T16:55:48ZRecent High-Resolution Structures of Amyloids Involved in Neurodegenerative Diseases1663-436510.3389/fnagi.2021.782617https://doaj.org/article/68da2e7d55264739ae58b2ab53218f2e2021-11-01T00:00:00Zhttps://www.frontiersin.org/articles/10.3389/fnagi.2021.782617/fullhttps://doaj.org/toc/1663-4365Amyloids are highly ordered aggregates composed of proteins or peptides. They are involved in several pathologies, including hallmark neurodegenerative disorders such as Alzheimer’s (AD) and Parkinson’s (PD). Individuals affected by these diseases accumulate in their brains amyloids inclusions composed of misfolded forms of a peptide (Aβ) and a protein (Tau) in AD and α-synuclein protein (α-Sn) in PD. Tau and α-Sn aggregates are also present in other neurodegenerative diseases. The insoluble nature and heterogeneity of amyloids have hampered their study at the molecular level. However, the use of solid state NMR and Cryogenic-electron microscopy along with fine-tuned modulation of the aggregation in vitro and improved isolation methods of brain-derived amyloids has allowed the elucidation of these elusive conformations at high resolution. In this work, we review the latest progress on the recent amyloid structures reported for Aβ, Tau, and α-Sn. The two-fold symmetry emerges as a convergent feature in the tridimensional arrangement of the protofilaments in the fibrillary structure of these pathological amyloids, with many of them exhibiting a Greek-key topology as part of their overall architecture. These specific features can serve as novel guides to seek potential molecular targets in drug design efforts.Rodrigo Diaz-EspinozaFrontiers Media S.A.articleneurodegenerative diseasesmisfoldingamyloidstructureAβTauNeurosciences. Biological psychiatry. NeuropsychiatryRC321-571ENFrontiers in Aging Neuroscience, Vol 13 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	neurodegenerative diseases misfolding amyloid structure Aβ Tau Neurosciences. Biological psychiatry. Neuropsychiatry RC321-571
spellingShingle	neurodegenerative diseases misfolding amyloid structure Aβ Tau Neurosciences. Biological psychiatry. Neuropsychiatry RC321-571 Rodrigo Diaz-Espinoza Recent High-Resolution Structures of Amyloids Involved in Neurodegenerative Diseases
description	Amyloids are highly ordered aggregates composed of proteins or peptides. They are involved in several pathologies, including hallmark neurodegenerative disorders such as Alzheimer’s (AD) and Parkinson’s (PD). Individuals affected by these diseases accumulate in their brains amyloids inclusions composed of misfolded forms of a peptide (Aβ) and a protein (Tau) in AD and α-synuclein protein (α-Sn) in PD. Tau and α-Sn aggregates are also present in other neurodegenerative diseases. The insoluble nature and heterogeneity of amyloids have hampered their study at the molecular level. However, the use of solid state NMR and Cryogenic-electron microscopy along with fine-tuned modulation of the aggregation in vitro and improved isolation methods of brain-derived amyloids has allowed the elucidation of these elusive conformations at high resolution. In this work, we review the latest progress on the recent amyloid structures reported for Aβ, Tau, and α-Sn. The two-fold symmetry emerges as a convergent feature in the tridimensional arrangement of the protofilaments in the fibrillary structure of these pathological amyloids, with many of them exhibiting a Greek-key topology as part of their overall architecture. These specific features can serve as novel guides to seek potential molecular targets in drug design efforts.
format	article
author	Rodrigo Diaz-Espinoza
author_facet	Rodrigo Diaz-Espinoza
author_sort	Rodrigo Diaz-Espinoza
title	Recent High-Resolution Structures of Amyloids Involved in Neurodegenerative Diseases
title_short	Recent High-Resolution Structures of Amyloids Involved in Neurodegenerative Diseases
title_full	Recent High-Resolution Structures of Amyloids Involved in Neurodegenerative Diseases
title_fullStr	Recent High-Resolution Structures of Amyloids Involved in Neurodegenerative Diseases
title_full_unstemmed	Recent High-Resolution Structures of Amyloids Involved in Neurodegenerative Diseases
title_sort	recent high-resolution structures of amyloids involved in neurodegenerative diseases
publisher	Frontiers Media S.A.
publishDate	2021
url	https://doaj.org/article/68da2e7d55264739ae58b2ab53218f2e
work_keys_str_mv	AT rodrigodiazespinoza recenthighresolutionstructuresofamyloidsinvolvedinneurodegenerativediseases
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Recent High-Resolution Structures of Amyloids Involved in Neurodegenerative Diseases

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