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The Effects of Lipids on α-Synuclein Aggregation In Vitro

The small neuronal protein α-synuclein (αS) is found in pre-synaptic terminals and plays a role in vesicle recycling and neurotransmission. Fibrillar aggregates of αS are the hallmark of Parkinson’s disease and related neurodegenerative disorders. In both health and disease, interactions with lipids...

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Autores principales: Ramirez, Jennifer, Pancoe, Samantha X., Rhoades, Elizabeth, Petersson, E. James
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10604467/
https://www.ncbi.nlm.nih.gov/pubmed/37892158
http://dx.doi.org/10.3390/biom13101476
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author Ramirez, Jennifer
Pancoe, Samantha X.
Rhoades, Elizabeth
Petersson, E. James
author_facet Ramirez, Jennifer
Pancoe, Samantha X.
Rhoades, Elizabeth
Petersson, E. James
author_sort Ramirez, Jennifer
collection PubMed
description The small neuronal protein α-synuclein (αS) is found in pre-synaptic terminals and plays a role in vesicle recycling and neurotransmission. Fibrillar aggregates of αS are the hallmark of Parkinson’s disease and related neurodegenerative disorders. In both health and disease, interactions with lipids influence αS’s structure and function, prompting much study of the effects of lipids on αS aggregation. A comprehensive collection (126 examples) of aggregation rate data for various αS/lipid combinations was presented, including combinations of lipid variations and mutations or post-translational modifications of αS. These data were interpreted in terms of lipid structure to identify general trends. These tabulated data serve as a resource for the community to help in the interpretation of aggregation experiments with lipids and to be potentially used as inputs for computational models of lipid effects on aggregation.
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spelling pubmed-106044672023-10-28 The Effects of Lipids on α-Synuclein Aggregation In Vitro Ramirez, Jennifer Pancoe, Samantha X. Rhoades, Elizabeth Petersson, E. James Biomolecules Review The small neuronal protein α-synuclein (αS) is found in pre-synaptic terminals and plays a role in vesicle recycling and neurotransmission. Fibrillar aggregates of αS are the hallmark of Parkinson’s disease and related neurodegenerative disorders. In both health and disease, interactions with lipids influence αS’s structure and function, prompting much study of the effects of lipids on αS aggregation. A comprehensive collection (126 examples) of aggregation rate data for various αS/lipid combinations was presented, including combinations of lipid variations and mutations or post-translational modifications of αS. These data were interpreted in terms of lipid structure to identify general trends. These tabulated data serve as a resource for the community to help in the interpretation of aggregation experiments with lipids and to be potentially used as inputs for computational models of lipid effects on aggregation. MDPI 2023-10-02 /pmc/articles/PMC10604467/ /pubmed/37892158 http://dx.doi.org/10.3390/biom13101476 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Ramirez, Jennifer
Pancoe, Samantha X.
Rhoades, Elizabeth
Petersson, E. James
The Effects of Lipids on α-Synuclein Aggregation In Vitro
title The Effects of Lipids on α-Synuclein Aggregation In Vitro
title_full The Effects of Lipids on α-Synuclein Aggregation In Vitro
title_fullStr The Effects of Lipids on α-Synuclein Aggregation In Vitro
title_full_unstemmed The Effects of Lipids on α-Synuclein Aggregation In Vitro
title_short The Effects of Lipids on α-Synuclein Aggregation In Vitro
title_sort effects of lipids on α-synuclein aggregation in vitro
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10604467/
https://www.ncbi.nlm.nih.gov/pubmed/37892158
http://dx.doi.org/10.3390/biom13101476
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