The mechanism of interaction between norfloxacin (NRF) and ciprofloxacin (CPF) with bovine serum albumin has been investigated using circular dichroism, fluorescence and absorption spectroscopy. The quenching mechanism of fluorescence of bovine serum albumin by fluoroquinolones was discussed. The binding sites number n and apparent binding constant K were measured by fluorescence quenching method. The thermodynamic parameters obtained from data at different temperatures were calculated. The distance r between donor (bovine serum albumin) and acceptor (fluoroquinolones) was obtained according to Forster theory of non-radiation energy transfer. The effect of common ions on binding constant was also investigated. The results of synchronous fluorescence spectra, UV-vis absorption spectra and circular dichroism of BSA in presence of fluoroquinolones show that the conformation of bovine serum albumin changed.
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