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Influence of the Ring Size on the Binding Ability of FTO Investigated by Fluorescence Spectroscopy

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Abstract

The fat mass and obesity associated protein (FTO) is a potential target for anti-obesity medicines. In this paper, we have synthesized two potential inhibitors for FTO, three-member-ring compound (W 3 ) and four-member-ring compound (W 4 ). The interactions of fat mass and obesity-associated (FTO) protein with W 3 (or W 4 ) have been studied by spectral method. Results show the intrinsic fluorescence is quenched by the W 3 (or W 4 ). The thermodynamics parameters indicate hydrophobic interaction play a major role in the interactions. The results of synchronous fluorescence spectra demonstrate that the microenvironments of Trp residue of FTO are disturbed by W 3 and W 4 . Results showed that W 3 are stronger quenchers and bind to FTO with the higher affinity than W 4 . The influence of molecular structure on the binding aspects has been investigated.

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Acknowledgments

We are grateful to the National Natural Science Foundation of China (#81330075) for financial support.

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    Authors and Affiliations

    1. College of Chemistry and Molecular Engineering, Zhengzhou University, 100 Science Avenue, Zhengzhou, 450001, People’s Republic of China

      Wu He, Zhigang Li, Lingling Yang, Qingwei Jiang, Ting Ren, Lijiao Zhang, Zhenhua Shen, Qinghua Yang, Ruiyong Wang & Junbiao Chang

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    1. Wu He
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    2. Zhigang Li
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    3. Lingling Yang
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    4. Qingwei Jiang
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    5. Ting Ren
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    6. Lijiao Zhang
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    7. Zhenhua Shen
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    8. Qinghua Yang
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    Corresponding authors

    Correspondence to Ruiyong Wang or Junbiao Chang.

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    Wu He and Zhigang Li contributed equally to this work.

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    He, W., Li, Z., Yang, L. et al. Influence of the Ring Size on the Binding Ability of FTO Investigated by Fluorescence Spectroscopy. J Fluoresc 25, 1655–1661 (2015). https://doi.org/10.1007/s10895-015-1652-8

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    • DOI: https://doi.org/10.1007/s10895-015-1652-8

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