Anionic nanoplastic contaminants promote Parkinson's disease-associated α-synuclein aggregation.
Recent studies have identified increasing levels of nanoplastic pollution in the environment. Here, we find that anionic nanoplastic contaminants potently precipitate the formation and propagation of α-synuclein protein fibrils through a high-affinity interaction with the amphipathic and non-amyloid component (NAC) domains in α-synuclein. Nanoplastics can internalize in neurons through clathrin-dependent endocytosis, causing a mild lysosomal impairment that slows the degradation of aggregated α-synuclein. In mice, nanoplastics combine with α-synuclein fibrils to exacerbate the spread of α-synuclein pathology across interconnected vulnerable brain regions, including the strong induction of α-synuclein inclusions in dopaminergic neurons in the substantia nigra. These results highlight a potential link for further exploration between nanoplastic pollution and α-synuclein aggregation associated with Parkinson's disease and related dementias.
Duke Scholars
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- alpha-Synuclein
- Parkinson Disease
- Microplastics
- Mice
- Inclusion Bodies
- Dopaminergic Neurons
- Animals
Citation
Published In
DOI
EISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- alpha-Synuclein
- Parkinson Disease
- Microplastics
- Mice
- Inclusion Bodies
- Dopaminergic Neurons
- Animals