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Comparison of the Quenching Effects of Two Main Components of Ziziphi Spinosae Semen on Serum Albumin Fluorescence

  • Baoai Wu
  • Chenhuan Qu
  • Yaxin Wang
  • Jinfeng Zhao
  • Huizhi DuEmail author
ORIGINAL ARTICLE
  • 18 Downloads

Abstract

Swertisin (6-glucosyl flavonoid) and spinosin (2″-β-O-glucopyranosyl swertisin) are two main components from Ziziphi Spinosae Semen, with anti-anxiety and hypnosis effects. The paper aims to compare the differences between the two compounds binding with serum albumins (BSA and HSA). Swertisin and spinosin statically quench intrinsic fluorescence of serum proteins by binding to proteins to form complexes. The fluorescence quenching rates of BSA induced by swertisin or spinosin are faster than those of HSA resulted by swertisin or spinosin, respectively. Each serum protein has only one binding site respectively accessible to the two compounds. Hydrophobic force and hydrogen bond play the important roles during the biding process of swertisin with proteins, but van der Waals force and hydrogen bond are major driving forces for spinosin binding to proteins. Synchronous fluorescence data show that spinosin binds to BSA and HSA and thus changes Tyr and Trp residue microenvironments, and has a greater effect on the latter. Compared with swertisin, spinosin has a stronger effect on the α-helix of proteins. But the distance between swertisin and proteins is slightly closer than spinosin. These findings will contribute to further understand the reaction of Ziziphi Spinosae Semen in the liver phase I oxidation, intestinal hydrolysis and deparaffin metabolism.

Keywords

Swertisin Spinosin Human serum albumin Bovine serum albumin Fluorescence quenching 

Notes

Acknowledgements

This work was supported by National Natural Science Foundation of China (No. 81403130), Shanxi Scholarship Council of China (No. 2017-021) and Natural Science Foundation of Shanxi Province (No. 201801D121290).

Compliance with Ethical Standards

Conflict of Interest

The authors claim that they have no conflict of interest.

Supplementary material

10895_2019_2422_MOESM1_ESM.doc (508 kb)
ESM 1 (DOC 508 kb)

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

Authors and Affiliations

  1. 1.School of Physical EducationShanxi UniversityTaiyuanChina
  2. 2.Institute of Molecular ScienceShanxi UniversityTaiyuanChina

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