Abstract
Thyroid disrupting chemicals (TDCs) can compete for the binding sites of transport proteins with thyroid hormones (THs) and alter the homeostasis of THs. The halogen moieties in TDCs play key role in determining the interactions between TDCs and transthyretin (TTR). Herein, the effects of halogenation on the binding interaction was investigated by analyzing the TTR crystal structures, the TDCs-TTR complex from molecular simulation, and the relative competing potency of a chemical with T 4 binding to hTTR (log RP ). We found that the halogen moieties in TDCs can affect the binding interactions by forming halogen bonds and halogen-hydrogen bonds with TTR and through inductive effects and hydrophobic effects. The halogen bonds (mainly halogen-oxygen bonds) and halogen-hydrogen bonds enhance the binding between organic halogenated compounds and TTR. Besides, for the halogenated phenolic compounds, the inductive effect is a main factor determining the log RP values. The hydrophobic effect is a critical factor governing the interactions between non-ionizable compounds (e.g. polybrominated diphenyl ethers) and TTR.
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