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International Journal of Analytical Chemistry
Volume 2012, Article ID 408057, 8 pages
Research Article

Interaction of Avelox with Bovine Serum Albumin and Effect of the Coexistent Drugs on the Reaction

Key Laboratory of Medical Chemistry and Molecular Diagnosis, College of Chemistry & Environmental Science, Hebei University, Ministry of Education, Baoding 071002, China

Received 7 September 2011; Accepted 15 November 2011

Academic Editor: Stig Pedersen-Bjergaard

Copyright © 2012 Baosheng Liu et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


The interaction between Avelox and bovine serum albumin (BSA) was investigated at different temperatures by fluorescence spectroscopy. Results showed that Avelox could quench the intrinsic fluorescence of BSA strongly, and the quenching mechanism was a static quenching process with Förester spectroscopy energy transfer. The electrostatic force played an important role on the conjugation reaction between BSA and Avelox. The order of magnitude of binding constants () was 104, and the number of binding site () in the binary system was approximately equal to 1. The binding distance () was less than 3 nm and the primary binding site for Avelox was located in subdomain IIA of BSA. Synchronous fluorescence spectra clearly revealed that the microenvironment of amino acid residues and the conformation of BSA were changed during the binding reaction. In addition, the effect of some antibiotics on the binding constant of Avelox with BSA was also studied.