Acta Phys. -Chim. Sin. ›› 2005, Vol. 21 ›› Issue (07): 792-795.doi: 10.3866/PKU.WHXB20050718

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Study on the Interaction between Cefodizime Sodium and Bovine Serum Albumin

SHAO Shuang; MA Bo-ying; WANG Xue-jie; ZHANG Jia-jie; LI Xue-feng; QIN Qing   

  1. Department of Chemistry, Zhejiang Education Institute, Hangzhou 310012; Matieria Medical Insitute of Hebei Province, Shijiazhuang 050061
  • Received:2004-12-07 Revised:2005-02-28 Published:2005-07-15
  • Contact: SHAO Shuang E-mail:sshao@zjei.net

Abstract: The binding reaction between cefodizime sodium (CDZM) and bovine serum albumin (BSA) in aqueous solution was studied by fluorescence spectra. The binding constant KA was found to be 5.31×104 and the binding sits n to be 0.94 at 299 K by fluorescence quenching method. The quenching mechanism of fluorescence of BSA by cefodizime sodium has been discussed. The thermodynamic parameters of binding reaction were determined as follows: the molar change of enthalpy ΔrHm=-15.8 kJ•mol-1, the molar change of Gibbs function ΔrGm=-27.0 kJ•mol-1 and the molar change of entropy ΔrSm=-90.0 J•K-1•mol-1, and the binding power between cefodizime sodium and bovine serum albumin has been considered. Furthermore, the binding distance (r=3.13 nm) between cefodizime sodium and bovine serum albumin was obtained according to the theory of Föster′s dipile-dipile non-radiation energy transfer mechanism, and the effect of cefodizime sodium on the conformation of bovine serum albumin was analyzed using synchronous fluorescence spectrometry.

Key words: Cefodizime sodium, Bovine serum albumin, Fluorescence quenching