The Effects of Lipids on α-Synuclein Aggregation In Vitro

Author:

Ramirez Jennifer1,Pancoe Samantha X.2,Rhoades Elizabeth23,Petersson E. James23ORCID

Affiliation:

1. Graduate Group in Biochemistry and Molecular Biophysics, Perelman School of Medicine, University of Pennsylvania, 421 Curie Boulevard, Philadelphia, PA 19104, USA

2. Department of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, PA 19104, USA

3. Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, 421 Curie Boulevard, Philadelphia, PA 19104, USA

Abstract

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.

Funder

National Institutes of Health

Publisher

MDPI AG

Subject

Molecular Biology,Biochemistry

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