Study of the interaction between sodium salts of (2E)-3-(4'-halophenyl)prop-2-enoyl sulfachloropyrazine and bovine serum albumin by fluorescence spectroscopy
Article first published online: 12 APR 2012
Copyright © 2012 John Wiley & Sons, Ltd.
Volume 28, Issue 2, pages 202–210, March/April 2013
How to Cite
Luo, X., Du, C., Wei, J., Deng, J., Lin, Y. and Lin, C. (2013), Study of the interaction between sodium salts of (2E)-3-(4'-halophenyl)prop-2-enoyl sulfachloropyrazine and bovine serum albumin by fluorescence spectroscopy. Luminescence, 28: 202–210. doi: 10.1002/bio.2364
- Issue published online: 19 APR 2013
- Article first published online: 12 APR 2012
- Manuscript Accepted: 16 FEB 2012
- Manuscript Revised: 9 FEB 2012
- Manuscript Received: 18 DEC 2011
- National Natural Science Foundation of China. Grant Number: 20962002, 20662001
- halo-cinnamic acid;
- bovine serum albumin;
- fluorescence spectroscopy;
Three sodium salts of (2E)-3-(4'-halophenyl)prop-2-enoyl sulfachloropyrazine (CCSCP) were synthesized and their structures were determined by 1H and 13C NMR, LC-MS and IR. The binding properties between CCSCPs and bovine serum albumin (BSA) were studied using fluorescence spectroscopy in combination with UV–vis absorbance spectroscopy. The results indicate that the fluorescence quenching mechanisms between BSA and CCSCPs were static quenching at low concentrations of CCSCPs or combined quenching (static and dynamic) at higher CCSCP concentrations of 298, 303 and 308 K. The binding constants, binding sites and corresponding thermodynamic parameters (ΔH, ΔS, ΔG) were calculated at different temperatures. All ΔG values were negative, which revealed that the binding processes were spontaneous. Although all CCSCPs had negative ΔH and positive ΔS, the contributions of ΔH and ΔS to ΔG values were different. When the 4'-substituent was fluorine or chlorine, van der Waals interactions and hydrogen bonds were the main interaction forces. However, when the halogen was bromine, ionic interaction and proton transfer controlled the overall energetics. The binding distances between CCSCPs and BSA were determined using the Förster non-radiation energy transfer theory and the effects of CCSCPs on the conformation of BSA were analyzed by synchronous fluorescence spectroscopy. Copyright © 2012 John Wiley & Sons, Ltd.