File:Hypothetical model for the pathological interaction between α-synuclein and nanoplastic contaminants in neurons.jpg

English: "Nanoparticles that have the intrinsic capacity to disrupt and cross the blood-brain barrier, such as small charged polystyrene particles, may come into contact with neurons that express high levels of α-synuclein and can harbor aggregates in disease. Peripheral cells susceptible to α-synuclein aggregation and outside of the blood-brain barrier (e.g., vagal neurons) may also come into contact with nanoplastic contaminants. Both α-synuclein fibrils and nanoplastics can enter the endolysosomal compartment in neurons through a clathrin-dependent endocytosis process. A healthy lysosome might fully degrade an α-synuclein aggregate. However, if a lysosome is impaired by nanoplastic particles, α-synuclein aggregates might not degrade and endogenous α-synuclein trafficked to the lysosome may inadvertently spur the formation of new α-synuclein fibrils through the potent pro-aggregation catalytic action of nanoplastics. This feedforward pathway highlights a two-part proposed mechanism whereby nanoplastic contaminants may accelerate the formation of misfolded α-synuclein in the endolysosome compartment and simultaneously impair the degradative action of the organelles (i.e., lysosomes) primarily responsible for their clearance."