Abstract
The interaction between ranitidine hydrochloride (RAN) and bovine serum albumin (BSA) in aqueous solution was investigated by means of fluorescence, synchronous fluorescence, and UV-Vis spectroscopy. The fluorescence of BSA was quenched remarkably by RAN and the quenching mechanism was concluded to be static quenching. The binding constants K and the number of binding sites n were calculated at three different temperatures. The RAN–BSA binding distance was determined to be less than 8 nm, suggesting that energy transfer may occur from BSA to RAN. The interaction process is spontaneous. Based on the obtained thermodynamic parameters, electrostatic forces may play a major role in this process. In addition, the effect of RAN on the conformation of BSA was analyzed using synchronous fluorescence spectra.
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He, LL., Wang, X., Liu, B. et al. Interaction Between Ranitidine Hydrochloride and Bovine Serum Albumin in Aqueous Solution. J Solution Chem 39, 654–664 (2010). https://doi.org/10.1007/s10953-010-9537-6
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DOI: https://doi.org/10.1007/s10953-010-9537-6