Acta Phys. -Chim. Sin. ›› 2009, Vol. 25 ›› Issue (07): 1342-1346.doi: 10.3866/PKU.WHXB20090706

• ARTICLE • Previous Articles     Next Articles

Effecting of Metal Ions on the Interaction between Zidovudine and Bovine Serum Albumin

SHAO Shuang, QIU Jin   

  1. Department of Chemistry, Zhejiang Education Institute, Hangzhou 310012, P. R. China|Department of Chemistry, Hangzhou Normal University, Hangzhou 310036, P. R. China
  • Received:2009-01-06 Revised:2009-03-23 Published:2009-06-26
  • Contact: SHAO Shuang


The interaction between zidovudine (ZDV) and bovine serum albumin (BSA) was investigated by fluorescence spectroscopy and ultraviolet-visible spectroscopy in aqueous solution (Tris-HCl buffer, pH 7.1). The effect of metal ions (Cu2+, Mg2+, Zn2+) on the interaction was also investigated. Results showed that the fluorescence intensity of BSA at 346 nm was quenched when zidovudine or metal ions were added. The quenching mechanism was a static quenching mechanism. A strong interaction exists between zidovudine and BSA. The thermodynamic parameters △H and △S were -10.2 kJ·mol-1 and 77.5 J·mol-1·K-1 at 298 K, respectively, indicating that electro-static forces played a major role. The binding constant, the number of binding site and the binding distance were 6.92×105 L·mol-1, 1.18, and 2.28 nm at 298 K, respectively. The binding constant and the number of binding sites decreased with the increase in temperature. The metal ions, Cu2+, Mg2+ and Zn2+, all decreased the binding constant and increased the binding distance for binding between ZDV and BSA.

Key words: Bovine serumalbumin, Zidovudine, Metal ion, Fluorescence quenching