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The Effect of Polyethylene Terephthalate Nanoplastics on Amyloid-β Peptide Fibrillation
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Lab experiments showed that PET nanoplastics, the type found in plastic bottles and clothing, accelerated the clumping of amyloid-beta proteins, which is a hallmark of Alzheimer's disease. Smaller nanoplastics (50 nm) had a stronger effect than larger ones, cutting the time for protein clumping nearly in half. While this is a test-tube study, it raises the question of whether nanoplastics that reach the brain could potentially speed up the development of Alzheimer's-related protein buildup.
Exposure of organisms to nanoplastics (NPs) is inevitable given their global abundance and environmental persistence. Polyethylene terephthalate (PET) is a common plastic used in a wide range of products, including clothing and food and beverage packaging. Recent studies suggest that NPs can cross the blood-brain barrier and cause potential neurotoxicity. It is widely known that aggregation of amyloid beta (Aβ) peptides in the brain is a pathological hallmark of Alzheimer's disease (AD). While the impact of nanoplastics such as polystyrene (PS) on amyloid aggregation has been studied, the effects of PET NPs remain unexplored. In this study, we examined the effect of PET NPs of different sizes (PET50nm and PET140nm) and concentrations (0, 10, 50, and 100 ppm) on the fibrillation of Aβ1-40. Our results showed that the presence of PET50nm as well as PET140nm decreased the lag phase of the fibrillation processes in a dose- and size-dependent manner from 6.7 ± 0.08 h for Aβ in the absence of PET (Aβcontrol) to 3.1 ± 0.03 h for PET50nm and 3.8 ± 0.06 h for PET140nm. CD spectroscopy showed that PET50nm significantly impacts the structural composition of Aβ aggregates. A significant rise in antiparallel β-sheet content and β-turn structure and a substantial reduction in other structures were observed in the presence of 100 ppm PET50nm. These changes indicate that higher concentrations (100 ppm) of PET50nm promote more rigid and uniform peptide aggregates. Although PET50nm NPs influence the kinetics of aggregation and secondary structure, the overall morphology of the resulting fibrils remains largely unaltered, as seen using transmission electron microscopy. Also, the local cross-β structure of the fibrils was not affected by the presence of PET50nm NPs during fibrillation, as confirmed using 13C solid-state NMR spectroscopy. Overall, these findings show that PET NPs accelerate amyloid fibril formation and alter the secondary structure of Aβ fibrils. These results also indicate that the accumulation of PET-NPs in the brain may facilitate the progression of various neurodegenerative diseases, including Alzheimer's disease.
More Papers Like This
The Effect of Polyethylene Terephthalate Nanoplastics on Amyloid-β Peptide Fibrillation
AI summary Read the abstract
Researchers investigated whether PET nanoplastics (50 nm and 140 nm) affect the fibrillation of amyloid-beta peptides associated with Alzheimer's disease pathology. PET nanoplastics at concentrations of 10–100 ppm influenced Aβ aggregation kinetics in a size- and concentration-dependent manner, adding to evidence that nanoplastics reaching the brain may modulate neurodegenerative protein aggregation.
Micro/NanoplasticsDrive Amyloid-β Colloidaland Oxidative Reorganization: A Real-World Contaminant Stressor
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Scientists tested how tiny plastic particles from everyday plastic bottles (PET plastic) interact with amyloid-beta, a protein linked to Alzheimer's disease, in lab experiments. They found these microplastics did change the protein's shape and behavior over time and slightly increased oxidative stress (a type of cell damage), but the exact real-world implications aren't yet clear. This early-stage research suggests microplastics could potentially influence processes involved in Alzheimer's disease, but more studies are needed before we know what this means for actual human health risk.
Impact of nanoplastics on Alzheimer ’s disease: Enhanced amyloid-β peptide aggregation and augmented neurotoxicity
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Researchers found that even very low concentrations of polystyrene nanoplastics can speed up the clumping of amyloid-beta protein, a hallmark of Alzheimer's disease, and increase its toxicity to brain cells. The hydrophobic (water-repelling) surface of the nanoplastics helps the proteins stick together faster, suggesting a potential link between environmental nanoplastic exposure and increased risk of Alzheimer's disease.
Evidence for protein misfolding in the presence of nanoplastics
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Computer simulations suggest that nanoplastics — tiny plastic particles under 5 nanometers — can cause proteins to misfold when they bind together. Misfolded proteins are linked to diseases like Alzheimer's, making this an early warning that nanoplastics may pose risks at the molecular level in living cells.
Nanoplastics forming micro-sized agglomerates and exacerbating neurotoxicity in Alzheimer's disease
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Tiny plastic particles (nanoplastics) can stick to the sticky amyloid plaques found in Alzheimer's disease, clumping together into larger particles that build up in the brain. In lab and mouse studies, this combo made brain cells more stressed and damaged, and worsened Alzheimer's-like symptoms in mice. This suggests that everyday plastic exposure—from food, water, and other sources—could potentially make Alzheimer's disease worse, though more research is needed to confirm this happens the same way in humans.
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