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Anionic nanoplastic contaminants promote Parkinson’s disease–associated α-synuclein aggregation
Summary
Researchers discovered that nanoplastics can enter brain cells and accelerate the clumping of alpha-synuclein, a protein whose buildup is the hallmark of Parkinson's disease. In mice, nanoplastics worsened the spread of this protein pathology across brain regions, including the area that controls movement, suggesting a potential link between nanoplastic pollution and Parkinson's disease risk.
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.