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Anionic Nanoplastic Contaminants Promote Parkinson’s Disease-Associated α-Synuclein Aggregation
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Researchers discovered that anionic nanoplastic contaminants can promote the formation and spread of alpha-synuclein protein fibrils, which are associated with Parkinson's disease. The study found that nanoplastics enter neurons, impair lysosomal function, and in mouse models, exacerbate the spread of alpha-synuclein pathology across brain regions, including dopaminergic neurons, highlighting a potential link between nanoplastic exposure and neurodegenerative processes that warrants further investigation.
Abstract 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.
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