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61,005 resultsShowing papers similar to Abstract 1036 A Biochemical Investigation on the Structural Integrity of Bovine Serum Albumin During Exposure to Plastic Particles
ClearElucidating the leaching effect of micro-/nano-plastics on the binding, structural, and oxidative characteristics of bovine serum albumin and its impact on cytotoxicity and oxidative stress in the human lung cancer cell line A549
Researchers examined how micro- and nanoplastics interact with bovine serum albumin, a key blood protein, and what happens when the altered protein contacts human lung cancer cells. They used biophysical methods and molecular docking to characterize how the plastic particles change the protein's structure and binding properties. The study found that protein-nanoplastic complexes showed increased toxicity and oxidative stress in lung cells compared to either component alone.
Bovine Serum Albumin Bends Over Backward to Interact with Aged Plastics: A Model for Understanding Protein Attachment to Plastic Debris
Scientists studied how proteins attach to plastic debris at different stages of sun-induced aging and found that weathered plastics attract significantly more protein binding and bacterial biofilm formation. The proteins physically reshape themselves to accommodate changes in the plastic's surface as it degrades. This matters because microplastics coated with biological material can more easily carry harmful bacteria and toxins through water systems and potentially into the human food chain.
Nanoplastics alter the conformation and activity of human serum albumin
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.
New insights into the toxic interactions of polyvinyl chloride microplastics with bovine serum albumin
Researchers investigated the binding interaction between polyvinyl chloride microplastics and bovine serum albumin using multiple spectroscopic techniques, finding that PVC MPs bind to BSA through hydrophobic interactions and alter the protein's secondary structure, suggesting potential implications for protein function in biological systems.
Probing the toxic interactions between polyvinyl chloride microplastics and Human Serum Albumin by multispectroscopic techniques
Scientists used multiple spectroscopic techniques to characterize how PVC microplastics interact with human serum albumin (the most abundant protein in blood), finding that PVC binds to albumin, alters its structure, and may affect the protein's ability to carry drugs and nutrients.
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.
Enhanced Macrophage Internalization of Photoaged Nanoplastics Mediated by Altered Serum Albumin Secondary Structure
Researchers found that nanoplastics exposed to sunlight in water undergo surface changes that alter how they interact with blood proteins, specifically human serum albumin. The aged nanoplastics caused the protein to unfold and change its structure, which in turn made immune cells take up the plastic particles more readily. The study suggests that environmental aging of nanoplastics could increase their biological activity and potential health effects once they enter the body.
Ovalbumin interaction with polystyrene and polyethylene terephthalate microplastics alters its structural properties
Researchers investigated how polystyrene and polyethylene terephthalate microplastics interact with ovalbumin, a common egg protein, under different pH conditions. They found that the microplastics adsorbed the protein and altered its three-dimensional structure, with smaller particles and acidic conditions leading to stronger interactions. The study suggests that microplastic contamination in food could change the structural properties of dietary proteins, potentially affecting how they are digested.
Polystyrene Nanoplastic Contaminants Denature Human Apolipoprotein A-1
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.
New molecular mechanism of nanoplastics affecting cadmium protein toxicity: Conformational response and differential binding of human serum albumin
Researchers showed that cadmium alone disrupts the structure and transport function of human serum albumin (the blood's main protein carrier), and that co-exposure with nanoplastics — which form a protein corona by binding albumin to their surface — further exacerbates these structural disruptions and enzyme activity losses, raising concerns about combined nanoplastic-heavy metal toxicity.
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.
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.
Size-Dependent Interactions of Degraded PET Nanoparticles with Human Serum Albumin: Thermodynamic and Molecular Insights
Researchers examined how degraded PET nanoparticles of different sizes interact with human serum albumin, a key protein in blood. They found that smaller, more degraded particles bind more strongly to the protein due to chemical changes on their surface, potentially altering the protein's structure and function. The study provides insights into how weathered plastic nanoparticles may behave once they enter the human body.
The carrier effect of polyethylene terephthalate microplastics in 4-methylimidazole and bovine serum albumin interactions
Researchers found that polyethylene terephthalate microplastics act as carriers for 4-methylimidazole, a food processing-derived pollutant, with the microplastic-adsorbed contaminant altering the structural conformation of bovine serum albumin more severely than the contaminant alone, suggesting a 'Trojan horse' enhancement of toxicity.
Soft and Hard Interactions between Polystyrene Nanoplastics and Human Serum Albumin Protein Corona
The structure of protein coronas formed when polystyrene nanoplastics interact with human serum albumin (HSA) was analyzed, finding that nanoplastic size and pH influenced whether hard (irreversible) or soft (exchangeable) corona formed, with weak but size-dependent interactions occurring despite the overall low affinity. The study provides mechanistic insight into how nanoplastics may interact with blood proteins upon entering the human circulatory system.
Unveiling the Modification of Esterase-like Activity of Serum Albumin by Nanoplastics and Their Cocontaminants
Researchers investigated how polystyrene nanoplastics with different surface charges and sizes affect the enzymatic activity of human serum albumin, a key blood protein. The study found that amino-modified and smaller nanoplastics had the greatest impact on protein structure and inhibited its ability to metabolize compounds, while the presence of the drug metformin reduced nanoplastic binding to the protein. These findings suggest that nanoplastics could interfere with normal protein function in the bloodstream and that co-exposure with other chemicals may alter how nanoplastics are transported in the body.
Molecular mechanism underlying the modulated toxicity of differently charged and sized nanoplastics by bovine serum albumin
This study examined how bovine serum albumin modulates the toxicity of polystyrene nanoplastics with different charges and sizes in biological systems. Serum albumin formed a protein corona that reduced the toxicity of negatively charged nanoplastics but had less protective effect against positively charged particles.
Enhanced MacrophageInternalization of Photoaged NanoplasticsMediated by Altered Serum Albumin Secondary Structure
Researchers found that photoaging of polystyrene nanoplastics in aquatic environments causes them to bind human serum albumin more avidly, and that this protein corona on photoaged NPs enhanced their internalization by macrophages compared to unaged particles.
Adsorption of clarithromycin on polystyrene nanoplastics surface and its combined adverse effect on serum albumin
Researchers examined how the antibiotic clarithromycin binds to the surface of polystyrene nanoplastics and how this combination interacts with blood proteins. They found that the drug readily adsorbed onto the nanoplastic surface and that the drug-nanoplastic complex altered the structure and function of serum albumin more than either substance alone. The findings suggest that nanoplastics could amplify the biological effects of pharmaceutical pollutants by acting as carriers in the body.
Proteins in contact with macro and microplastics : fate in solution and at interfaces
This French doctoral thesis investigated how proteins interact with plastic surfaces and microplastic particles in solution and at interfaces. The research found that proteins can adsorb to plastic surfaces, potentially altering both protein function and plastic behavior. These findings have implications for understanding how microplastics interact with biological molecules in the human body and environment.
The weakened physiological functions of human serum albumin in presence of polystyrene nanoplastics
Researchers found that polystyrene nanoplastics interfere with human serum albumin, the most abundant protein in blood that performs critical functions like transporting substances and acting as an enzyme. The nanoplastics reduced the protein's enzyme activity and altered its ability to transport chemicals like bisphenol A. This study provides evidence that once nanoplastics enter the human bloodstream, they could disrupt important blood protein functions with potential health consequences.
Influence of protein configuration on aggregation kinetics of nanoplastics in aquatic environment
Researchers investigated how five different proteins with varying structures affect the aggregation behavior of polystyrene nanoplastics in water under different ionic strength and pH conditions. They found that protein type and configuration significantly influenced whether nanoplastics clumped together or remained dispersed, with globular proteins like albumin having different effects than fibrous proteins like collagen. The study suggests that the protein composition of natural waters plays an important role in determining how nanoplastics behave and transport in aquatic environments.
Synergistic Effect of Nanoplastics and GenX on Human Serum Albumin: The Role of Protein Corona Formation and Co-Adsorption
Researchers investigated how nanoplastics interact with human serum albumin (HSA) in the presence of GenX—an emerging PFAS replacement chemical—using spectroscopy and molecular docking. The protein corona formed on nanoplastics altered GenX binding to albumin in a synergistic way, suggesting that nanoplastics can amplify PFAS bioavailability by disrupting their normal protein interactions in blood.
Microplastics Interact with β-lactoglobulin: Implications for Protein Structure, Digestibility, and Allergenicity
Researchers studied how microplastics commonly released from baby bottles interact with the major milk allergen beta-lactoglobulin. The study found that polypropylene, polyethersulfone, and polyphenylsulfone microplastics altered the protein's structure, which may affect its digestibility and allergenic properties, raising potential concerns for infants with cow's milk allergy.