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Evidence-Based Complementary and Alternative Medicine
Volume 2014 (2014), Article ID 247595, 12 pages
Research Article

The Spectroscopy Study of the Binding of an Active Ingredient of Dioscorea Species with Bovine Serum Albumin with or without Co2+ or Zn2+

1Key Laboratory of Development and Application of Forest Chemicals of Guangxi, Guangxi University of Nationalities, Nanning 530006, China
2Key Laboratory for the Chemistry and Molecular Engineering of Medicinal Resources (Ministry of Education of China), School of Chemistry and Pharmaceutical Sciences of Guangxi Normal University, Guilin 541004, China

Received 30 March 2014; Revised 6 May 2014; Accepted 15 May 2014; Published 4 June 2014

Academic Editor: Shi-Biao Wu

Copyright © 2014 He-Dong Bian et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Diosgenin (DIO) is the active ingredient of Dioscorea species. The interaction of DIO with bovine serum albumin (BSA) was investigated through spectroscopic methods under simulated physiological conditions. The fluorescence quenching data revealed that the binding of DIO to BSA without or with Co2+ or Zn2+ was a static quenching process. The presence of Co2+ or Zn2+ both increased the static quenching constants KSV and the binding affinity for the BSA-DIO system. In the sight of the competitive experiment and the negative values of ΔH0 and ΔS0, DIO bound to site I of BSA mainly through the hydrogen bond and Van der Waals’ force. In addition, the conformational changes of BSA were studied by Raman spectra, which revealed that the secondary structure of BSA and microenvironment of the aromatic residues were changed by DIO. The Raman spectra analysis indicated that the changes of conformations, disulfide bridges, and the microenvironment of Tyr, Trp residues of BSA induced by DIO with Co2+ or Zn2+ were different from that without Co2+ or Zn2+.