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: Narmin Bashirova, Franziska Schölzel, Dominik Hornig, Holger A. Scheidt, Martin Krueger, Georgeta Salvan, Daniel Huster, Joerg Matysik, A. Alia
Format: Article
Language:English
Published: MDPI AG 2025-03-01
Series:Molecules
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Online Access:https://www.mdpi.com/1420-3049/30/7/1432
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author Narmin Bashirova
Franziska Schölzel
Dominik Hornig
Holger A. Scheidt
Martin Krueger
Georgeta Salvan
Daniel Huster
Joerg Matysik
A. Alia
author_facet Narmin Bashirova
Franziska Schölzel
Dominik Hornig
Holger A. Scheidt
Martin Krueger
Georgeta Salvan
Daniel Huster
Joerg Matysik
A. Alia
author_sort Narmin Bashirova
collection DOAJ
description 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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spelling doaj-art-29e4fb1dd0ea46c3b2ae6d906ded1edb2025-08-20T03:08:55ZengMDPI AGMolecules1420-30492025-03-01307143210.3390/molecules30071432The Effect of Polyethylene Terephthalate Nanoplastics on Amyloid-β Peptide FibrillationNarmin Bashirova0Franziska Schölzel1Dominik Hornig2Holger A. Scheidt3Martin Krueger4Georgeta Salvan5Daniel Huster6Joerg Matysik7A. Alia8Institute of Medical Physics and Biophysics, Leipzig University, D-04107 Leipzig, GermanyInstitute of Physics, Chemnitz University of Technology, D-09126 Chemnitz, GermanyCenter for Materials, Architectures and Integration of Nanomembranes, Chemnitz University of Technology, D-09126 Chemnitz, GermanyInstitute of Medical Physics and Biophysics, Leipzig University, D-04107 Leipzig, GermanyInstitute of Anatomy, Leipzig University, D-04107 Leipzig, GermanyInstitute of Physics, Chemnitz University of Technology, D-09126 Chemnitz, GermanyInstitute of Medical Physics and Biophysics, Leipzig University, D-04107 Leipzig, GermanyInstitute of Analytical Chemistry, Leipzig University, D-04103 Leipzig, GermanyInstitute of Medical Physics and Biophysics, Leipzig University, D-04107 Leipzig, GermanyExposure 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.https://www.mdpi.com/1420-3049/30/7/1432polyethylene terephthalatenanoplasticsamyloid βfibrillation
spellingShingle Narmin Bashirova
Franziska Schölzel
Dominik Hornig
Holger A. Scheidt
Martin Krueger
Georgeta Salvan
Daniel Huster
Joerg Matysik
A. Alia
The Effect of Polyethylene Terephthalate Nanoplastics on Amyloid-β Peptide Fibrillation
Molecules
polyethylene terephthalate
nanoplastics
amyloid β
fibrillation
title The Effect of Polyethylene Terephthalate Nanoplastics on Amyloid-β Peptide Fibrillation
title_full The Effect of Polyethylene Terephthalate Nanoplastics on Amyloid-β Peptide Fibrillation
title_fullStr The Effect of Polyethylene Terephthalate Nanoplastics on Amyloid-β Peptide Fibrillation
title_full_unstemmed The Effect of Polyethylene Terephthalate Nanoplastics on Amyloid-β Peptide Fibrillation
title_short The Effect of Polyethylene Terephthalate Nanoplastics on Amyloid-β Peptide Fibrillation
title_sort effect of polyethylene terephthalate nanoplastics on amyloid β peptide fibrillation
topic polyethylene terephthalate
nanoplastics
amyloid β
fibrillation
url https://www.mdpi.com/1420-3049/30/7/1432
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