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20 resultsShowing papers similar to Plastic Nanoparticles Cause Proteome Stress and Aggregation by Compromising Cellular Protein Homeostasis ex vivo and in vivo.
ClearPlastic nanoparticles cause proteome stress and aggregation by compromising cellular protein homeostasis ex vivo and in vivo
Researchers found that polystyrene nanoplastics — even at levels that don't kill cells — can destabilize the entire protein network inside cells and organs, causing widespread protein misfolding and clumping (aggregation) that standard liver function tests completely miss. In mice, nanoplastics accumulating in the liver also reduced the organ's ability to process drugs like acetaminophen, raising concerns about hidden health effects from long-term nanoplastic exposure.
Mechanistic Insights into Cellular and Molecular Basis of Protein‐Nanoplastic Interactions
This review examines how nanoplastic particles interact with proteins at the cellular and molecular level, disrupting normal protein function and triggering oxidative stress, DNA damage, and cell death. Researchers found that nanoplastics alter the structural shape of important proteins, which helps explain their toxic effects on living organisms. The study also covers how understanding these protein-plastic interactions could inform both toxicity assessment and potential enzymatic plastic degradation strategies.
Evidence for protein misfolding in the presence of nanoplastics
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 can change the secondary structure of proteins
Researchers found that nanoplastic particles interact directly with proteins and fundamentally alter their secondary structure, effectively denaturing them in a manner that could cause cellular and ecological damage. The study presents the first direct evidence that plastic-protein interactions represent a distinct and potentially serious biological hazard beyond the previously studied effects of microplastic ingestion.
Micro- and Nanoplastics’ Effects on Protein Folding and Amyloidosis
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.
Interfacial interactions between PMMA nanoplastics and a model globular protein: towards a molecular understanding of nanoplastic-driven biological dyshomeostasis
Researchers investigated the molecular interactions between PMMA nanoplastics and a model globular protein to understand how nanoplastics disrupt normal protein function. They found that PMMA nanoplastics bind to and alter the structural conformation of the protein, potentially contributing to cellular protein dysfunction.
Exploring the Interaction of Human α-Synuclein with Polyethylene Nanoplastics: Insights from Computational Modeling and Experimental Corroboration
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.
Elucidating the Neurotoxicopathological Impact of Micro and Nanoplastics: Mechanistic Insights Into Oxidative Stress-mediated Neurodegeneration and Implications for Public Health in a Plastic Pervasive Era
Researchers reviewed the growing evidence linking micro- and nanoplastic exposure to neurodegenerative diseases, identifying oxidative stress, neuroinflammation, DNA damage, and protein misfolding as key mechanisms of harm to the brain. The review highlights critical knowledge gaps — especially around chronic low-dose exposure — and calls for better detection tools and public health policies to address the emerging neurological threat from plastic pollution.
Impact of nanoplastics on Alzheimer ’s disease: Enhanced amyloid-β peptide aggregation and augmented neurotoxicity
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.
Polystyrene nanoplastics affect the human ubiquitin structure and ubiquitination in cells: a high-resolution study
Using NMR and TEM analyses, polystyrene nanoplastics were shown to form a hard protein corona with human ubiquitin and to impair ubiquitination in HeLa cells, revealing a potential mechanism by which nanoplastic exposure disrupts protein degradation pathways in human cells.
Aggregation Kinetics and Stability of Biodegradable Nanoplastics: Effects of Weathering and Proteins
Researchers studied how weathering and proteins affect the aggregation and stability of biodegradable nanoplastics in water. Biodegradable plastics can still generate persistent nanoscale particles that behave differently depending on environmental conditions, complicating assumptions about their safety compared to conventional plastics.
Fluorogenic Hyaluronan Nanogels Track Individual Early Protein Aggregates Originated under Oxidative Stress
Not relevant to microplastics — this study presents fluorogenic hyaluronan nanogels that can detect and visualize early protein aggregation events in real time, with applications in understanding diseases associated with misfolded proteins.
Assessment on interactive prospectives of nanoplastics with plasma proteins and the toxicological impacts of virgin, coronated and environmentally released-nanoplastics
Researchers found that nanoplastics quickly coat themselves in blood proteins, forming a multi-layered "corona" that changes the proteins' shape and makes them biologically harmful; these protein-coated nanoplastics caused more DNA and cell damage in human blood cells than bare nanoplastics. The study highlights the need to regulate nanoplastics in medical products and better understand how they accumulate in the body.
Unraveling Intracellular Protein Corona Components of Nanoplastics via Photocatalytic Protein Proximity Labeling
Researchers developed a photocatalytic protein proximity labeling method to identify proteins that interact with nanoplastic particles inside living cells. The study revealed the composition of the intracellular protein corona that forms around nanoplastics, providing new insights into how these tiny plastic particles interact with cellular machinery once they enter biological systems.
Protein aggregation, hydrophobicity and neurodegenerative disease
This doctoral thesis on protein aggregation and neurodegenerative disease includes an important finding relevant to microplastics: nanoscale PET plastic particles were shown to accelerate the formation of amyloid fibrils from alpha-synuclein, a protein central to Parkinson's disease. This raises the concern that everyday nanoplastic exposure could contribute to the onset or progression of neurodegenerative conditions.
Aging Processes Dramatically Alter the Protein Corona Constitution, Cellular Internalization, and Cytotoxicity of Polystyrene Nanoplastics
Researchers found that aging processes such as UV and ozone exposure dramatically alter how polystyrene nanoplastics interact with blood plasma proteins, form protein coronas, and enter cells. The study suggests that environmentally aged nanoplastics may have different biological effects than pristine particles, which has important implications for accurately assessing the health risks of real-world nanoplastic exposure.
Role of the Protein Corona in the Colloidal Behavior of Microplastics
Researchers investigated how protein coronas form on polyethylene and polypropylene microplastics in biological media, finding that proteins act as surfactants that alter the colloidal behavior and stability of microplastics in aquatic environments.
Microplastic Exposure Promotes Amyloid Misfolding and Metabolic Impairment at Sub-Lethal Doses in an In Vitro Cellular Model of Alzheimer’s Disease
Researchers exposed cellular models of Alzheimer's disease to sub-lethal polystyrene microplastics and nanoplastics and monitored amyloid protein misfolding and metabolic impairment using photothermal microscopy. Even low-dose plastic exposure promoted amyloid aggregation and disrupted cellular energy metabolism, suggesting microplastics may accelerate the molecular processes underlying Alzheimer's pathology.
Molecular insights into nanoplastics-peptides binding and their interactions with the lipid membrane
Using computer simulations, researchers studied how nanoplastics interact with small protein fragments and cell membranes at the molecular level. They found that nanoplastics readily bind to proteins, forming a coating called a protein corona, which changes how the plastics behave when they encounter cell membranes. This research helps explain how nanoplastics might enter human cells, since the protein coating could either help or hinder the particles from crossing biological barriers.
Exploring the Impact of Microplastics and Nanoplastics on Macromolecular Structure and Functions
This review explores how micro- and nanoplastics interact with the building blocks of our cells, including proteins, fats, and DNA. The plastics can cause oxidative stress, disrupt hormones, damage genetic material, cause proteins to misfold, and destabilize cell membranes. The authors propose that these effects are interconnected through feedback loops that could accelerate cellular aging and potentially pass harmful changes to future generations.