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The mechanism and conformational changes of polybrominated diphenyl ethers to TTR by fluorescence spectroscopy,

Jie Xu1, Yuchen Wei, Wu Yang

  • 1Guangxi Colleges and Universities Key Laboratory of Food Safety and Detection; College of Chemistry and Bioengineering, Guilin University of Technology, Guilin 541004, China. yzs@glut.edu.cn.

The Analyst
|September 4, 2018
PubMed

Insights

Polybrominated diphenyl ethers (PBDEs) bind to transthyretin (TTR), a protein linked to diseases. This interaction, primarily hydrophobic and involving cation-π bonding with LYS15, impacts TTR stability and function.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Toxicology

Background:

  • Transthyretin (TTR) aggregation is implicated in human diseases affecting the nervous system and organs.
  • Polybrominated diphenyl ethers (PBDEs) are environmental contaminants with potential health impacts.

Purpose of the Study:

  • To elucidate the interaction mechanism between TTR and specific PBDEs (BDE49, BDE108, BDE155).
  • To understand the role of TTR residue LYS15 in PBDE binding and its implications for TTR function.

Main Methods:

  • Spectroscopic techniques (steady-state fluorescence, time-resolved fluorescence, UV-Vis spectroscopy).
  • Computational methods (molecular docking, thermodynamic analysis, quantum chemistry).

Main Results:

  • PBDEs induce fluorescence quenching in TTR via static quenching and Förster's resonance energy transfer.
  • Binding is primarily hydrophobic, involving cation-π interactions between PBDEs and TTR's LYS15 residue.
  • Specific PBDEs exhibit significant energy contributions to LYS15, enhancing binding stability.

Conclusions:

  • The LYS15 residue in TTR is critical for its interaction with PBDEs.
  • PBDE binding to TTR, particularly via LYS15, may influence TTR's physiological roles and disease association.
  • Understanding these interactions provides insights into PBDE toxicity and TTR-related pathologies.

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