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20 resultsShowing papers similar to Study on the binding of polystyrene microplastics with superoxide dismutase at the molecular level by multi-spectroscopy methods
ClearSize-dependent effects of nanoplastics on structure and function of superoxide dismutase
Researchers used multi-spectroscopic techniques to examine how nanoplastics of different sizes interact with and alter the structure and function of the antioxidant enzyme superoxide dismutase. The study found size-dependent effects, with nanoplastics binding to the enzyme and altering its secondary structure, ultimately reducing its activity, which has implications for understanding how nanoplastics may disrupt cellular antioxidant defenses.
Probing the molecular mechanism of interaction between polystyrene nanoplastics and catalase by multispectroscopic techniques
Researchers investigated the molecular mechanism of interaction between polystyrene nanoplastics and the antioxidant enzyme catalase using multispectroscopic techniques, revealing how nanoplastic accumulation may disrupt enzymatic function and contribute to oxidative stress.
Spectroscopic investigations on the interaction between nano plastic and catalase on molecular level
Researchers investigated how polystyrene nanoplastics interact with the enzyme catalase at different pH levels, finding that nanoplastics alter the protein's secondary structure and reduce its enzymatic activity through static quenching and hydrophobic binding mechanisms.
Multispectroscopic Investigations of the Binding Interaction between Polyethylene Microplastics and Human Hemoglobin
Scientists used multiple spectroscopic techniques to investigate whether polyethylene microplastics can bind to human hemoglobin, the protein that carries oxygen in blood. They found that microplastic particles do interact with hemoglobin, altering its structural shape and potentially affecting its function. The findings raise questions about what might happen when microplastics enter the human bloodstream and interact with essential blood proteins.
Molecular mechanisms of polystyrene nanoplastics and alpha-amylase interactions and their binding model: A multidimensional analysis
This study investigated how polystyrene nanoplastics bind to alpha-amylase, an important digestive enzyme that breaks down starches. The nanoplastics attached to the enzyme, changed its shape, and reduced its activity, potentially interfering with normal digestion. If nanoplastics consumed through food and water impair digestive enzymes in a similar way inside the human body, it could affect how well we break down and absorb nutrients from our meals.
Induced structural changes of humic acid by exposure of polystyrene microplastics: A spectroscopic insight
Researchers used spectroscopic methods to investigate how polystyrene microplastics interact with dissolved organic matter at the molecular level. They found that microplastics bind to the aromatic structures of humic acid through chemical bonding, forming a highly conjugated co-polymer complex with altered structural properties. The study reveals that microplastics can fundamentally change the chemistry of natural organic matter in aquatic environments, which may affect pollutant transport and biogeochemical cycles.
Probing the molecular interaction between photoaged polystyrene microplastics and fulvic acid
Researchers investigated how photoaged polystyrene microplastics interact with fulvic acid, a common natural organic compound found in water environments. Using advanced spectroscopy techniques, they found that aging changed the surface chemistry of the microplastics and altered how they bind to fulvic acid at the molecular level. The study suggests that weathering processes in the environment may significantly change how microplastics interact with and transport other dissolved substances in water.
Multispectroscopy analysis of polystyrene nanoplastic interaction with diastase α-amylase
Researchers used fluorescence spectroscopy and other analytical techniques to characterize how polystyrene nanoplastics bind to and alter the structure of alpha-amylase, a key digestive enzyme, suggesting nanoplastic exposure could potentially disrupt starch digestion.
Enhanced binding of triclocarban to catalase induced by coexisting nanoplastics
Researchers showed that polystyrene nanoplastics worsen the binding of the antimicrobial compound triclocarban to the antioxidant enzyme catalase by forming a protein corona on the nanoplastic surface and distorting the enzyme's 3D structure, leading to greater-than-expected overactivation of catalase activity and heightened oxidative stress compared to triclocarban exposure alone.
Assessment of polystyrene nano plastics effect on human salivary α-amylase structural alteration: Insights from an in vitro and in silico study
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.
Characterizing the binding interactions between virgin/aged microplastics and catalase in vitro
Researchers compared how virgin and UV-aged PVC microplastics interact with the antioxidant enzyme catalase in laboratory conditions. The study found that aged microplastics had more binding sites and caused greater structural changes to the enzyme, including loosening of protein chains, though neither form affected the enzyme's core activity since the particles were too large to enter the enzyme's interior.
Evidence of microplastics release from polythene and paper cups exposed to hot and cold: A case study on the compromised kinetics of catalase
Researchers found that both polythene bags and paper cups release microplastic particles when exposed to hot and cold water at various time intervals. The study demonstrated that these released microplastics can bind to and alter the structure of the antioxidant enzyme catalase, reducing its enzymatic activity by approximately 1.4-fold, suggesting that everyday plastic-containing materials may release particles that interfere with biological processes.
Effect of polystyrene microplastic and chlorpyrifos pesticide on superoxide dismutase activity in tissues of rainbow trout (Oncorhynchus mykiss)
Rainbow trout were exposed to polystyrene microplastics, the pesticide chlorpyrifos, and a combination of both, with researchers measuring effects on antioxidant enzyme activity. The combined exposure caused greater disruption to superoxide dismutase activity than either pollutant alone, suggesting microplastics can amplify pesticide toxicity in fish.
Polystyrene microplastics sunlight-induce oxidative dissolution, chemical transformation and toxicity enhancement of silver nanoparticles
Researchers discovered that polystyrene microplastics can induce sunlight-driven oxidative dissolution and chemical transformation of silver nanoparticles, enhancing their toxicity and revealing important implications for how co-occurring pollutants interact in the environment.
Spectroscopic Investigation of Increased Fluorescent Intensity of Fluorescent Dyes When Adsorbed onto Polystyrene Microparticles
Researchers investigated how fluorescent dyes used to stain and identify microplastics behave differently depending on the plastic polymer type and surrounding water chemistry. Understanding how staining conditions affect fluorescence intensity helps improve the reliability of dye-based microplastic detection methods.
Determination of bioaccumulation of polystyrene nanoplastics in mussel Mytilus galloprovincialis and their impact on enzymatic and nonenzymatic antioxidative stress mechanisms
Researchers assessed the bioaccumulation of polystyrene nanoplastics in the mussel Mytilus galloprovincialis and measured enzymatic and non-enzymatic antioxidant stress responses after 4 days of exposure to 1 mg/L of 54 nm particles. Nanoplastics accumulated in mussel tissues and triggered significant oxidative stress responses, including altered superoxide dismutase and catalase activity, indicating toxicological effects at environmentally relevant concentrations.
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.
Insights into the Binding Interactions between Microplastics and Human α-Synuclein Protein by Multispectroscopic Investigations and Amyloidogenic Oligomer Formation
Researchers found that common microplastics -- especially polystyrene -- can bind to alpha-synuclein, a brain protein whose clumping is a hallmark of Parkinson's disease. The microplastics altered the protein's structure and promoted the formation of toxic clumps called amyloidogenic oligomers. This suggests that microplastic exposure could potentially accelerate the protein misfolding process linked to Parkinson's and other neurodegenerative diseases.
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.
Nanoplastics composite norfloxacin induced changes in conformation and function of lysozyme and differential effects of co-exposure contamination
Researchers used spectroscopy and molecular docking to show that nanoplastics and the antibiotic norfloxacin form stable co-aggregates that bind near the active site of lysozyme, reducing its enzymatic activity by nearly 40% and altering the protein's secondary structure more severely than either contaminant alone.