The Effect of Polyethylene Terephthalate Nanoplastics on Amyloid-β Peptide Fibrillation
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 t...
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| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2025-03-01
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| Series: | Molecules |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1420-3049/30/7/1432 |
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| Summary: | 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 (PET<sub>50nm</sub> and PET<sub>140nm</sub>) and concentrations (0, 10, 50, and 100 ppm) on the fibrillation of Aβ<sub>1-40</sub>. Our results showed that the presence of PET<sub>50nm</sub> as well as PET<sub>140nm</sub> 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 (Aβ<sub>control</sub>) to 3.1 ± 0.03 h for PET<sub>50nm</sub> and 3.8 ± 0.06 h for PET<sub>140nm</sub>. CD spectroscopy showed that PET<sub>50nm</sub> 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 PET<sub>50nm</sub>. These changes indicate that higher concentrations (100 ppm) of PET<sub>50nm</sub> promote more rigid and uniform peptide aggregates. Although PET<sub>50nm</sub> 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 PET<sub>50nm</sub> NPs during fibrillation, as confirmed using <sup>13</sup>C 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. |
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| ISSN: | 1420-3049 |