Environmental Science and Pollution Research

, Volume 19, Issue 7, pp 2528–2536 | Cite as

Binding of triclosan to human serum albumin: insight into the molecular toxicity of emerging contaminant

  • Jiabin Chen
  • Xuefei Zhou
  • Yalei Zhang
  • Yanqin Zi
  • Yajie Qian
  • Haiping Gao
  • Shuangshuang Lin
15th International Symposium on Toxicity Assessment

Abstract

Purpose

The interaction between triclosan (TCS) and human serum albumin (HSA) was investigated in order to obtain the binding mechanism, binding constant, the type of binding force, the binding distance between the donor and acceptor, and the effect of TCS on the conformation change of HSA.

Methods

A HSA solution was added to the quartz cell and then titrated by successive addition of TCS. The fluorescence quenching spectra and synchronous spectra were recorded with the excitation and emission slits of the passage of band set at 10 and 20 nm. Three-dimensional fluorescence spectra of HSA were recorded before and after the addition of TCS. The capillary electrophoresis was conducted with the pressure injection mode at 0.5 psi for 5 s, separation under 25 kV, and detection at 214 nm.

Results

Fluorescence data indicated the fluorescence quenching of HSA by TCS was static quenching, and the quenching constants (Ka) were 1.14 × 105, 8.75 × 104, 6.67 × 104, and 5.00 × 104 at 293, 298, 303, and 309 K, respectively. The thermodynamic parameters, enthalpy change (ΔH) and entropy change (ΔS) for the interaction were calculated to be −37.9 kJ mol−1 and 32.6 J mol−1 K−1. The binding distance between TCS and tryptophan residues of HSA was obtained to be 1.81 nm according to Fǒrster nonradioactive energy transfer theory. The UV-Vis absorption spectroscopy, the synchronous fluorescence spectroscopy, three-dimensional fluorescence spectroscopy, and circular dichroism spectroscopy revealed the alterations of HSA secondary structure in the presence of TCS. Finally, the interaction between TCS and HSA was further confirmed by capillary electrophoresis.

Conclusions

TCS was bound to HSA to form the TCS-HSA complex, with the binding distance of 1.81 nm. Hydrophobic interaction and hydrogen bond were dominated in the binding. TCS could change the secondary conformation of HSA. This work provides an insight into noncovalent interaction between emerging pollutants and protein, helping to elucidate the toxic mechanism of such pollutants.

Keywords

HSA Triclosan Noncovalent interaction Fluorescence Capillary electrophoresis 

Notes

Acknowledgments

We sincerely thank the National Natural Science Foundation of China (41072172), State Key Laboratory of Pollution Control and Resource Reuse (Tongji University), China (no. PCRRY 11001), the Transformation Fund for Agricultural Science and Technology Achievements of the Ministry of Science and Technology, China (2010GB23600672), and the Research Foundation of Shanghai Committee of Science and Technology (10595312500) for financially supporting this work.

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Copyright information

© Springer-Verlag 2012

Authors and Affiliations

  • Jiabin Chen
    • 1
  • Xuefei Zhou
    • 2
  • Yalei Zhang
    • 1
  • Yanqin Zi
    • 3
  • Yajie Qian
    • 2
  • Haiping Gao
    • 2
  • Shuangshuang Lin
    • 1
  1. 1.State Key Laboratory of Pollution Control and Resources Reuse, College of Environmental Science and EngineeringTongji UniversityShanghaiChina
  2. 2.Key Laboratory of Yangtze River Water Environment for Ministry of Education College of Environmental Science and EngineeringTongji UniversityShanghaiChina
  3. 3.Department of Chemistry and Material ScienceHuaibei Normal UniversityHuaibeiChina

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