Journal of Solution Chemistry

, Volume 48, Issue 11–12, pp 1519–1534 | Cite as

Probing the Binding of Bicyclol and Human Serum Albumin by Multispectral Technologies and Molecular Docking Method

  • Cai Liu
  • Yan Zhang
  • Jingjing Guo
  • Fengling CuiEmail author


In this paper, under the condition of a simulated human physiological environment, steady-state fluorescence, UV spectra, three-dimensional fluorescence, time-resolved fluorescence, and the circular dichroism were implemented to investigate the binding mechanism between bicyclol (BYL) and human serum albumin (HSA). The results revealed a red shift in the UV absorption wavelength of HSA and an increase in absorption intensity of HSA with increasing concentration of bicyclol. Bicyclol quenched the intrinsic fluorescence of HSA via a static quenching mechanism. At 298 K, the number of binding sites (n) and binding constant of BYL–HSA were about 1 and 9.67 × 103 L·mol−1, respectively. The thermodynamic parameters ΔG, ΔH, ΔS are − 22.76 and − 19.07 kJ·mol−1 and 27.17 J·K−1·mol−1 respectively, which demonstrated that the binding of bicyclol and HSA was mainly driven by hydrophobic and electrostatic forces. In addition, the molecular docking method was utilized to further investigate the binding site when BYL is combined with HSA, which indicated that BYL is bound on the hydrophobic cavities of sub-domains IIA and IIIA of HSA, respectively, and that the binding affinity in the IIIA site was much higher than that in the IIA site.


Human serum albumin Bicyclol Multispectral technologies Molecular docking Binding mechanism 



Thanks to Dr. Yan Zhang for her great contribution to this article.


This study was funded by National Natural Science Foundation of China–Union Foundation of Henan (U1704170), National Natural Science Foundation of China (21605041), Key Programs of Henan for Science and Technology Development (182102310103, 182102310848, and 192102310300), the Program for Innovative Research Team in University of Henan Province (18IRTSTHN003).

Compliance with ethical standards

Conflict of interest

There is no conflict of interest.


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Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2019

Authors and Affiliations

  • Cai Liu
    • 1
  • Yan Zhang
    • 1
  • Jingjing Guo
    • 1
  • Fengling Cui
    • 1
    Email author
  1. 1.Collaborative Innovation Center of Henan Province for Green Manufacturing of Fine Chemicals, Key Laboratory of Green Chemical Media and Reactions, Ministry of Education, National Demonstration Center for Experimental Chemistry Education, Henan Engineering Laboratory for Bioconversion Technology of Functional Microbes, School of Chemistry and Chemical EngineeringHenan Normal UniversityXinxiangPeople’s Republic of China

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