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Molecular mechanisms of ciprofloxacin-loaded nanoplastics on human serum albumin: Protein denaturation and binding site recognition
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Scientists found that when tiny plastic particles (nanoplastics) team up with the antibiotic ciprofloxacin, the combo does more damage to a key blood protein called human serum albumin than either substance does alone, warping its shape and blocking its normal function. This matters because albumin helps carry nutrients, drugs, and hormones through your bloodstream, so this lab study suggests that pollution "cocktails" of plastics and antibiotics in the environment could pose a compounded health risk that we haven't been accounting for.
Nanoplastics (NPs) and antibiotics are prevalent environmental pollutants that coexist and interact in the environment, leading to complex multi-level toxicities. However, there is currently insufficient research on the effects of co-exposure to polystyrene nanoplastics (PSNPs) and ciprofloxacin (CIP) on key human proteins, such as human serum albumin (HSA), and the interaction mechanisms and binding modes between them remain unclear. This study investigated the effects of CIP-loaded PSNPs (PSNPs@CIP) on HSA's function and structure and explored the binding mode through site competition and molecular docking. The results revealed that PSNPs@CIP inhibited HSA's esterase-like activity (62.0 %), more significantly than CIP (72.2 %) or PSNPs (87.0 %), indicating stronger functional disruption. Meanwhile, PSNPs@CIP caused more severe structural disruption of HSA, including alterations in backbone conformation, secondary structure, and the amino acid microenvironment. PSNPs@CIP interfered with the n→π* electronic transition of the peptide backbone (absorption reduced by 0.99, red shift 6.0 nm), and promoted the decrease of α-helix content to 47.3 %. A red shift of 9.8 nm (Δλ=60 nm) indicated an altered tryptophan (Trp) microenvironment. CIP preferentially binds to Sudlow site I of HSA via hydrogen bonding with Ala215, Lys199, and Lys195. This study demonstrates that PSNPs@CIP composite contamination aggravates HSA structural and functional impairment by promoting the direct binding of CIP to Sudlow site I and facilitating HSA adsorption onto PSNPs as a "protein corona". This study elucidates the molecular-level mechanisms and binding modes of PSNPs@CIP affecting HSA, providing crucial evidence for assessing NPs co-pollution and environmental behavior.
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Adsorption of clarithromycin on polystyrene nanoplastics surface and its combined adverse effect on serum albumin
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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.
Co-Existing Nanoplastics Further Exacerbates the Effects of Triclosan on the Physiological Functions of Human Serum Albumin
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Scientists found that when nanoplastics and triclosan (an antimicrobial chemical) are present together, the nanoplastics make triclosan bind more strongly to human serum albumin, a key blood protein. This stronger binding disrupts the protein's normal enzyme function more than triclosan alone would. The findings are concerning because people are exposed to both nanoplastics and triclosan simultaneously, and their combined effect on blood proteins could be worse than either substance individually.
Surface interaction of vancomycin with polystyrene microplastics and its effect on human serum albumin
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Researchers studied how the antibiotic vancomycin interacts with polystyrene microplastics and what happens when that combination encounters human blood proteins. They found that vancomycin readily adsorbs onto microplastic surfaces, and that the resulting particle-drug complex can alter how the antibiotic binds to serum albumin in the blood. The study suggests that microplastics in the body could interfere with how medications are transported and function in the bloodstream.
Interactions of nanoplastics with human albumin and hemoglobin: Structural and spectroscopic insights
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Scientists found that tiny plastic particles (nanoplastics) can physically attach to two key proteins in human blood, albumin and hemoglobin (the protein that carries oxygen), and actually change their shape. This matters because a protein's shape determines how well it works in the body, so these changes could potentially affect how blood proteins function, though more research is needed to confirm real-world health effects. It's an early but important clue in understanding how the plastic pollution we're increasingly exposed to might interact with our bodies at the molecular level.
Nanoplastics amplify ciprofloxacin-induced immunotoxicity: Oxidative stress in splenocytes and conformational and functional changes in lysozyme
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In lab tests on mouse spleen cells, nanoplastics combined with the antibiotic ciprofloxacin caused more oxidative stress, cell damage, and inflammation than ciprofloxacin alone. The combination also caused greater structural and functional changes to the immune protein lysozyme, suggesting nanoplastics may worsen ciprofloxacin's harmful effects on immune cells.
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