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• W4313573740 endingPage "964" @default.
• W4313573740 startingPage "964" @default.
• W4313573740 abstract "Biotransformation is recognized as a potential pathway to regulate the environmental risk of microcystins (MCs). To explore the regulation effectiveness and mechanism of the biotransformation pathway, six typical MCLR-biotransformation products (MCLR-BTPs) were prepared, and their inhibition effects on protein phosphatase 2A (PP2A) were evaluated. The inhibition effects of the MCLR-BTPs generally decreased with the increase in biothiol molecular weights and polarity, indicating that biotransformation was an effective pathway through which to regulate MCLR toxicity. To further explore the regulation mechanism, the key interaction processes between the MCLR/MCLR-BTPs and the PP2A were explored by homology modeling and molecular docking. The introduced biothiols blocked the covalent binding of Mdha7 to Cys269 but strengthened the hydrogen bond Mdha7→Arg268. The changed Mdha7 intervened the combination of MCLR-BTPs to PP2A by weakening the hydrogen bonds Arg4←Arg214, Arg4→Pro213, Adda5←His118, and Ala1←Arg268, and the ionic bond Glu6-Mn12+. The weakening combination of the MCLR-BTPs to PP2A further attenuated the interactions between the conserved domain and the Mn2+ ions (including the ionic bonds Asp57-Mn12+ and Asp85-Mn12+ and the metal bonds Asp57-Mn12+ and Asn117-Mn12+) and increased the exposure of the Mn2+ ions. Meanwhile, the weakened hydrogen bond Arg4←Arg214 facilitated the combination of the phosphate group to Arg214 (with increased exposure). In this way, the catalytic activity of the PP2A was restored." @default.
• W4313573740 created "2023-01-06" @default.
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• W4313573740 date "2023-01-05" @default.
• W4313573740 modified "2023-09-26" @default.
• W4313573740 title "Regulation Effectiveness and Mechanism of Biotransformation Pathway on the Toxicity of Microcystin-LR Target to Protein Phosphatase 2A" @default.
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• W4313573740 doi "https://doi.org/10.3390/ijerph20020964" @default.
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