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In silico study unveils catalase and superoxide dismutase-1 as the potential sub-cellular targets of microplastic-associated compounds and their relevance to oxidative stress
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Molecular docking analysis showed that microplastic-associated compounds—especially bisphenol A—bind strongly to the antioxidant enzymes catalase and superoxide dismutase-1, suggesting these chemicals can disrupt cellular oxidative stress defenses. This mechanistic insight explains how microplastic leachates may impair antioxidant function in tissues, providing a molecular basis for the oxidative stress and endocrine disruption effects observed in microplastic exposure studies.
Microplastic pollution has posed significant threats to the biosphere. They have been detected in human samples and are known to modulate endogenous antioxidants. However, the mechanism of action remains unclear. Hence, the present study aims to determine the docking affinities of microplastic-associated compounds, such as bisphenol A (BPA), methyl methacrylate (MMC), vinyl chloride (VC), and polyethylene terephthalate (PET), for catalase (CAT) and superoxide dismutase-1 (SOD1). Binding affinity and SwissADME analyses were performed. The tested compounds exhibited binding affinities for CAT in order of VC (-3.0 kcal/mol) < MMC (-4.4 kcal/mol) < PET (-6.8 kcal/mol) < BPA (-8.3 kcal/mol). Similarly, compounds showed binding affinity for SOD1 in order of VC (-2.2 kcal/mol) < MMC (-4.2 kcal/mol) < PET (-6.3 kcal/mol) < BPA (-7.2 kcal/mol). Hydrogen bonds, van der Waals forces, and hydrophobic interactions were observed. Compounds, except VC, were permeable through the gastrointestinal tract and the blood-brain barrier. Moreover, they followed Lipinski’s and Veber’s rule, indicating bioabsorption and distribution potentials. Therefore, results suggest that the tested microplastic-associated compounds can interact with CAT and SOD1 to modulate their functions and fuel oxidative stress. • Microplastic-associated compounds can target CAT and SOD1. • BPA, MMC, PET, and VC exhibited notable binding affinities for antioxidants. • H-bonds and hydrophobic interactions were apparent at the docked complex. • BPA, MMC, and PET were permeant to GI and BBB. • Altered catalytic functions of CAT and SOD1 might trigger oxidative stress.
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