Document Type
Article
Publication Date
2010
Digital Object Identifier (DOI)
https://doi.org/10.2174/1875039701003010001
Abstract
α-Synuclein (α-Syn) is a small intrinsically disordered presynaptic protein known to form insoluble filamentous inclusions in Parkinson’s disease (PD) and other neurodegenerative disorders. Various catecholamines can inhibit the α-Syn fibrillation in vitro. Recently, non-covalent binding of DOPAC (3,4-dihydroxyphenylacetic acid), a normal product of the dopamine metabolism, was shown to inhibit the fibrillation of α-Syn due to the DOPAC-induced stabilization of the normally transient oligomers thus preventing them from subsequent fibril formation (Zhou, et al. J. Mol. Biol. 2009, 388 (3), 597-610). We are showing here that the interaction of DOPAC with α-Syn decreases the binding affinity of α- Syn to lipids, suggesting that DOPAC might lead to the gain-of-toxicity of α-Syn aggregates and loss-of-function of α- Syn, both of which could be related to progression of PD.
Rights Information
This work is licensed under a Creative Commons Attribution-Noncommercial 3.0 License
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
The Open Proteomics Journal, v. 2010, issue 3, p. 1-7
Scholar Commons Citation
Zhou, Wenbo; Long, Chunmei; Fink, Anthony L.; and Uversky, Vladimir N., "3, 4-dihydroxyphenylacetic Acid (DOPAC) Impairs α-synuclein Interaction with Lipids" (2010). Molecular Medicine Faculty Publications. 544.
https://digitalcommons.usf.edu/mme_facpub/544
