Journal
JOURNAL OF LUMINESCENCE
Volume 130, Issue 12, Pages 2281-2287Publisher
ELSEVIER
DOI: 10.1016/j.jlumin.2010.07.005
Keywords
Oxybutynin hydrochloride; Bovine serum albumin; Fluorescence quenching; Displacement studies
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Funding
- Education Foundation of Liaoning Province, China [20060362]
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The mutual interaction of oxybutynin hydrochloride (OB) with bovine serum albumin (BSA) was investigated by fluorescence, UV-vis absorption, circular dichroism (CD), and Fourier transform infrared (FT-IR) spectroscopies under simulative physiological conditions. The results of fluorescence titration revealed that OB could quench the intrinsic fluorescence of BSA by static quenching and there was a single class of binding sites on BSA for this drug. The thermodynamic parameters Delta H, Delta S, and Delta G calculated at different temperatures indicated that hydrogen bonds and van der Waals interactions were the dominant intermolecular forces in stabilizing the OB-BSA complexes. According to the theory of Forster's non-radiation energy transfer, the binding distance r between OB and BSA was evaluated to be 3.27 nm. The displacement experiments confirmed that OB could bind to site I of BSA. The FT-IR and CD spectra showed that the binding of OB to BSA induced conformational changes in BSA. (C) 2010 Elsevier B.V. All rights reserved.
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