The Spectroscopy Study of the Binding of an Active Ingredient of Dioscorea Species with Bovine Serum Albumin with or without Co(2+) or Zn(2+).

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 Zn(2+) was a static quenching process. The presence of Co(2+) or Zn(2+) both increased the static quenching constants K SV and the binding affinity for the BSA-DIO system. In the sight of the competitive experiment and the negative values of ΔH (0) and ΔS (0), 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 Co(2+) or Zn(2+) were different from that without Co(2+) or Zn(2+).

Binding of engeletin with bovine serum albumin: insights from spectroscopic investigations.

In this paper, several spectroscopic techniques were used to investigate the interaction of engeletin (ELN) with bovine serum albumin (BSA). The analysis of UV-Vis absorption and fluorescence spectra revealed that ELN and BSA formed a static complex ELN-BSA, and ELN quenched the fluorescence of BSA effectively. According to the thermodynamic parameters ΔS(0) = 47.27 J·mol(-1)·K(-1) and ΔΗ(0) = -10.34 kJ·mol(-1), the hydrophobic and hydrogen bond interactions were suggested to be the major interaction forces between ELN and BSA. Raman spectroscopy indicated that the binding of ELN slightly changed the conformations and microenviroment of BSA and decreased the α-helix content of BSA.

Study on the structural changes of bovine serum albumin with effects on polydatin binding by a multitechnique approach.

Polydatin is a traditional Chinese medicine which shows effective biological activity as antimicrobial and antiviral agent. The secondary structure changes of bovine serum albumin (BSA) were investigated by the methods of Fourier transform infrared spectroscopy (FT-IR), circular dichroism (CD) and Raman spectroscopy. The experimental results indicated that polydatin changed the secondary structure of BSA. The presence of polydatin decreased α-helix content of BSA. The conformations of disulfide bridges and the microenvironment of Tyr, Trp residues were also changed.