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Interaction Between Ranitidine Hydrochloride and Bovine Serum Albumin in Aqueous Solution

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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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Authors and Affiliations

  1. College of Applied Chemistry, Shenyang Institute of Chemical Technology, Shenyang, 110142, P.R. China

    Ling-Ling He & Ya-Guang Sun

  2. School of Pharmaceutical Sciences, Liaoning University, Shenyang, 110036, P.R. China

    Xin Wang, Bin Liu & Jun Wang

Authors
  1. Ling-Ling He
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  2. Xin Wang
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  3. Bin Liu
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  4. Jun Wang
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Correspondence to Xin Wang.

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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

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