Chem. J. Chinese Universities

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Studies on Competitive Reaction Between Bovine Serum Albumin and Ampicillin with Evans Blue as Fluorescent Probe by Fluorescence Spectroscopy

ZHAO Hu1, PANG Yan-Ling2, ZHANG Min1, YUE Ning-Ning1, LÜ Qing-Luan1, ZHANG Miao1, WANG Huai-You1*   

    1. College of Chemistry, Chemical Engineering and Materials Science, Shandong Normal University, Jinan 250014, China;
    2. Department of Chemistry and Chemical Engineering, Heze College, Heze 274015, China
  • Received:2007-07-20 Revised:1900-01-01 Online:2008-03-10 Published:2008-03-10
  • Contact: WANG Huai-You

Abstract: The competitive reaction between ampicillin and bovine serum albumin(BSA) was studied with Evans blue(EB) as a fluorescence probe by the fluorescence spectroscopy. Fluorescence quenching occurred between the bovine serum albumin and Evans blue. The static fluorescence quenching process was confirmed on the basis of the Stern-Volmer plot. The binding constant(KBSA-EB=1.122×106 L/mol) and the number of binding sites(n=0.9935) were obtained. The enthalpy change, entropy change and free energy change were calculated, and the types of interaction force between EB and BSA were investigated. The relative fluorescence intensity of BSA was recovered gradually with increasing the concentration of ampicillin. The results indicate that there was a competitive interaction between ampicillin and EB for BSA, and the interaction mechanism was studied, the binding constant of EB with ampicillin, KEB-A=7.131×105 L/mol, was obtained.

Key words: Bovine serum albumin, Evans blue, Ampicillin, Fluorescence quenching

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