Journal
JOURNAL OF MOLECULAR STRUCTURE
Volume 970, Issue 1-3, Pages 128-133Publisher
ELSEVIER
DOI: 10.1016/j.molstruc.2010.02.061
Keywords
Dibazol; Bovine serum albumin (BSA); Fluorescence quenching; Resonance light scattering; FT-IR spectroscopy
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Funding
- National Nature Science Foundation of China [10172043]
- International Science and Technology Cooperation Program of Jiangsu Province of China [BZ2008060]
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The characteristics of the binding reaction of dibazol to bovine serum albumin (BSA) were investigated by fluorescence, UV-vis, resonance light scattering (RLS) and Fourier transform infrared (FT-IR) spectroscopy. Results show that dibazol causes the fluorescence quenching of BSA through a static quenching procedure. The binding constants for the formation of a complex between dibazol and BSA are 0.83, 1.23 and 1.62 x 10(5) mol(-1) L at 295, 302 and 309 K, respectively. Positive values of thermodynamic parameters namely enthalpy change (Delta H) and entropy change (Delta S) indicate that the interaction between dibazol and BSA is driven mainly by hydrophobic forces. It seems that the binding is spontaneous at standard state for the change in standard Gibbs free energy (Delta G) value is negative. The binding distance between BSA and dibazol was calculated to be about 4.28 nm according to the Forster theory. The site marker competitive experiments confirmed that the binding of dibazol to BSA primarily occurred in site I of BSA. In addition, the effect of dibazol on the conformation of BSA was also analyzed by using synchronous fluorescence and FT-IR spectroscopy. (C) 2010 Elsevier B.V. All rights reserved.
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