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PolystyreneNanoplastic Contaminants Denature HumanApolipoprotein A‑1
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This study found that polystyrene nanoplastics denature human apolipoprotein A-1 upon binding, altering the protein's structure in ways that could impair its function in cholesterol metabolism and HDL formation, raising concerns about nanoplastic effects on cardiovascular health.
The subject of nanoplastics is of growing importance, as the use of plastics in our everyday lives has caused nanoplastics to be abundant in the air, water, and soil, bringing them in contact with humans and animals. Understanding how proteins bind and structure themselves at these nanoplastic interfaces is critical for determining the toxicity and health implications of nanoplastics. Proteomics has determined the most abundant protein in human protein corona formed around nanoplastics; however, the structure and orientation of these proteins is extremely challenging to determine. We use in situ sum frequency scattering vibrational spectroscopy and two-dimensional infrared spectroscopy to probe the structure of human liver protein apolipoprotein A-1 (ApoA-1) when adsorbed to polystyrene (PS) nanoparticles. The spectra indicate that ApoA-1 aggregates and forms fibrillar structures at the PS nanoplastic interface, leading to clustering of PS nanoplastics, which may pose a significant risk to human health.
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Polystyrene Nanoplastic Contaminants Denature Human Apolipoprotein A-1
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Researchers used advanced spectroscopy techniques to study what happens when a key human blood protein, apolipoprotein A-1, comes into contact with polystyrene nanoplastics. They found that the protein changes its structure and forms abnormal fibrillar clumps at the nanoplastic surface, causing the plastic particles to cluster together. Since apolipoprotein A-1 is important for cholesterol transport, these structural changes at the nanoplastic interface may pose risks to cardiovascular health.
Nanoplastics alter the conformation and activity of human serum albumin
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Researchers investigated how polystyrene nanoplastics interact with human serum albumin, a key blood protein, and found that nanoplastics bind to the protein through hydrophobic forces, altering its structure and reducing its enzymatic activity. The study suggests that nanoplastic exposure could interfere with normal protein function in the bloodstream, highlighting the need for regulation of nanoplastics in consumer products.
Interaction of polystyrene nanoplastics with human fibrinogen
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Researchers found that polystyrene nanoplastics with different surface modifications disrupted the structure of human fibrinogen, a key blood clotting protein, in a dose-dependent manner. The study suggests that nanoplastics entering the bloodstream could interfere with protein function, raising concerns about the potential biological consequences of nanoplastic exposure in humans.
[Polystyrene nanoplastics disrupt macrophage cholesterol metabolism by adsorbing apolipoprotein E].
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Researchers used proteomic analysis combined with molecular docking and dynamics simulations to show that polystyrene nanoplastics selectively adsorb apolipoprotein E (APOE) in macrophages by occupying key binding residues, blocking APOE–cholesterol interaction and causing intracellular lipid accumulation—identifying a molecular mechanism that may explain how nanoplastic exposure promotes atherosclerosis risk.
Assessment of polystyrene nano plastics effect on human salivary α-amylase structural alteration: Insights from an in vitro and in silico study
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Researchers investigated how polystyrene nanoplastics interact with human salivary alpha-amylase, a key digestive enzyme, using both laboratory experiments and computer modeling. They found that the nanoplastics competitively inhibited the enzyme and caused structural changes including loss of secondary protein structure. The study suggests that nanoplastic exposure in the digestive system may interfere with normal enzyme function, raising concerns about potential impacts on human digestion.
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