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Exploring the mechanism of interaction between TBG and halogenated thiophenols: Insights from fluorescence analysis and molecular simulation.
Chen, Yanting; Liang, Wenhui; Huang, Muwei; Li, Cancan; Song, Zeyu; Zheng, Yanhong; Yi, Zhongsheng.
Afiliación
  • Chen Y; College of Chemistry and Bioengineering, Guilin University of Technology, Guilin 541004, China.
  • Liang W; College of Chemistry and Bioengineering, Guilin University of Technology, Guilin 541004, China.
  • Huang M; College of Chemistry and Bioengineering, Guilin University of Technology, Guilin 541004, China.
  • Li C; College of Chemistry and Bioengineering, Guilin University of Technology, Guilin 541004, China.
  • Song Z; College of Chemistry and Bioengineering, Guilin University of Technology, Guilin 541004, China.
  • Zheng Y; College of Chemistry and Bioengineering, Guilin University of Technology, Guilin 541004, China.
  • Yi Z; College of Chemistry and Bioengineering, Guilin University of Technology, Guilin 541004, China. Electronic address: yzs@glut.edu.cn.
Int J Biol Macromol ; 261(Pt 2): 129645, 2024 Mar.
Article en En | MEDLINE | ID: mdl-38296143
ABSTRACT
Thyroxine-binding globulin (TBG) plays a vital role in regulating metabolism, growth, organ differentiation, and energy homeostasis, exerting significant effects in various key metabolic pathways. Halogenated thiophenols (HTPs) exhibit high toxicity and harmfulness to organisms, and numerous studies have demonstrated their thyroid-disrupting effects. To understand the mechanism of action of HTPs on TBG, a combination of competitive binding experiments, multiple fluorescence spectroscopy techniques, molecular docking, and molecular simulations was employed to investigate the binding mechanism and identify the binding site. The competition binding assay between HTPs and ANS confirmed the competition of HTPs with thyroid hormone T4 for the active site of TBG, resulting in changes in the TBG microenvironment upon the binding of HTPs to the active site. Key amino acid residues involved in the binding process of HTPs and TBG were further investigated through residue energy decomposition. The distribution of high-energy contributing residues was determined. Analysis of root-mean-square deviation (RMSD) demonstrated the stability of the HTPs-TBG complex. These findings confirm the toxic mechanism of HTPs in thyroid disruption, providing a fundamental reference for accurately assessing the ecological risk of pollutants and human health. Providing mechanistic insights into how HTPS causes thyroid diseases.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fenoles / Compuestos de Sulfhidrilo / Tiroxina / Globulina de Unión a Tiroxina Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: Int J Biol Macromol Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Países Bajos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fenoles / Compuestos de Sulfhidrilo / Tiroxina / Globulina de Unión a Tiroxina Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: Int J Biol Macromol Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Países Bajos