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RETRACTED ARTICLE: In silico analysis of human CYP1A1 protein and microplastics interaction
Summary
Researchers used computer modeling to examine how eight common plastic types bind to CYP1A1, a key human enzyme that processes toxins in the body, finding that polycarbonate and polyethylene terephthalate showed the strongest binding. If microplastics interfere with CYP1A1 function, they could reduce the body's ability to detoxify other environmental chemicals — though lab and animal studies are still needed to confirm these effects. Note: this article has been retracted.
Microplastics (MPs) are ubiquitous environmental pollutants, raising significant concerns about their potential impacts on human health. Cytochrome P450 1A1 (CYP1A1) plays a crucial role in the biotransformation and detoxification of xenobiotics, including some pollutants. Understanding the interaction between MPs and CYP1A1 is critical, as altered CYP1A1 activity can have significant toxicological consequences. This study employed molecular docking to investigate the binding affinities and interactions of eight commonly encountered MPs (polystyrene, polymethyl methacrylate, polyvinyl chloride, polyethylene, polyurethane, polyethylene terephthalate, polychloroprene, and polycarbonate), representing a range of polymer types, with CYP1A1. Molecular docking of the MPs (structures obtained from PubChem) to CYP1A1 (PDB ID: 4I8V) was performed using PyRx. The binding affinities (ΔG kcal/mol) ranged from − 2.3 (polyethylene) to– 7.4 (polycarbonate), with the following ranking: polycarbonate (– 7.4) > polyethylene terephthalate (– 7.1) > polystyrene (– 6.8) > polymethyl methacrylate (– 4.7) > polychloroprene (– 4.5) > polyurethane (– 4.1) > polyvinyl chloride (– 2.8) > polyethylene (– 2.3) These results suggest that certain MPs have a higher propensity to bind to CYP1A1, indicating a potential for altered enzyme activity and subsequent toxicological effects related to altered CYP1A1 activity, such as increased susceptibility to other environmental toxins or disruption of normal metabolic processes. Hydrophobic interactions and hydrogen bonding were key contributors to the binding affinities. This study provides valuable insights into the potential interactions between MPs andCYP1A1, highlighting the need for further in vitro and in vivo research to understand the implications for human health and environmental impact.
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