publication . Article . 2010

Interaction Between Ranitidine Hydrochloride and Bovine Serum Albumin in Aqueous Solution

Yaguang Sun;
Restricted
  • Published: 11 May 2010 Journal: Journal of Solution Chemistry, volume 39, pages 654-664 (issn: 0095-9782, eissn: 1572-8927, Copyright policy)
  • Publisher: Springer Science and Business Media LLC
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...
Subjects
free text keywords: Physical and Theoretical Chemistry, Biophysics, Biochemistry, Molecular Biology
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