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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.
Abstract The possible effect of plastic nanoparticles of waste origin on biological systems is still unclear and could pose a severe threat. Model studies at the molecular level are urgently needed in order to help reveal the interplay between these particles and biological systems, and thereby to indicate the direction of further research. In the present study, simulated annealing molecular dynamics is adjusted and applied to generate an array of conformations for a sample peptide oligoalanine possibly binding to polyethylene and nylon 6,6 nanoplastics. The resulting structures, with a diameter of up to 5 nm, were investigated with the aid of static quantum chemical calculations. The obtained data unequivocally show that both plastic nanoparticles influence the relative stability of α ‐helix, β ‐hairpin, and other conformations strongly. Polyethylene nanoparticle increases the stability of the helical foldamer. Nylon 6,6 nanoplastic offers strong plastic‐peptide interactions on its surface, making the unfolding of the peptide thermodynamically highly favorable. These results further underscore that nanoplastics can do significant molecular‐level damage to living organisms via facilitating the misfolding and denaturation of proteins. Furthermore, it is apparent that plastics can have very different effects on living matter depending upon their composition, and hence experiments with any single kind of plastics (eg, polystyrene) should not be considered generally valid for all nanoplastics.
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Evidence for Protein Misfolding in the Presence of Nanoplastics
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Researchers used molecular dynamics simulations to demonstrate that nanoplastic particles can induce protein misfolding in biological systems. The study represents an early model-based investigation of how nanoplastics may interfere with protein structure and function at the molecular level.
Exploring the Interaction of Human α-Synuclein with Polyethylene Nanoplastics: Insights from Computational Modeling and Experimental Corroboration
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Researchers used computer simulations and lab experiments to study how polyethylene nanoplastics interact with alpha-synuclein, a brain protein linked to neurodegenerative conditions. They found that nanoplastics caused the protein to change its shape and form a compact structure that interacts more strongly with itself, potentially promoting clumping. The study suggests a possible mechanism by which nanoplastics could influence protein behavior in the brain, though the health implications remain to be determined.
Micro- and Nanoplastics’ Effects on Protein Folding and Amyloidosis
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This review examines how micro- and nanoplastic particles may interact with proteins in the body, potentially influencing protein folding and triggering the formation of abnormal amyloid structures. The study suggests that plastic particles can cross the blood-brain barrier in animal models and interact with neurons, raising questions about possible links between plastic exposure and protein misfolding conditions.
Plastic Nanoparticles Cause Proteome Stress and Aggregation by Compromising Cellular Protein Homeostasis ex vivo and in vivo.
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Researchers demonstrated for the first time that plastic nanoparticles can compromise cellular protein homeostasis ex vivo and in vivo, causing proteome stress and protein aggregation by disrupting the cellular machinery responsible for maintaining protein stability. The findings suggest that nanoplastic exposure poses risks beyond cytotoxicity, potentially triggering protein misfolding pathways relevant to neurodegenerative and other protein aggregation diseases.
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.
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