The spectroscopy study of the binding of an active ingredient of Dioscorea species with bovine serum albumin with or without co2+ or zn 2+

Abstract

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 Co 2+ or Zn2+ was a static quenching process. The presence of Co2+ or Zn2+ both increased the static quenching constants Kand 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 Co 2+ or Zn2+. © 2014 He-Dong Bian et al.