Insights into In Vitro Binding of Parecoxib to Human Serum Albumin by Spectroscopic Methods
Article first published online: 17 JUN 2014
© 2014 Wiley Periodicals, Inc.
Journal of Biochemical and Molecular Toxicology
Volume 28, Issue 10, pages 433–441, October 2014
How to Cite
Shang, S., Liu, Q., Gao, J., Zhu, Y., Liu, J., Wang, K., Shao, W. and Zhang, S. (2014), Insights into In Vitro Binding of Parecoxib to Human Serum Albumin by Spectroscopic Methods. J. Biochem. Mol. Toxicol., 28: 433–441. doi: 10.1002/jbt.21582
- Issue published online: 6 OCT 2014
- Article first published online: 17 JUN 2014
- Manuscript Accepted: 13 MAY 2014
- Manuscript Revised: 8 MAY 2014
- Manuscript Received: 18 MAR 2014
- Human Serum Albumin;
- Circular Dichroism;
- Molecular Docking
Herein, we report the effect of parecoxib on the structure and function of human serum albumin (HSA) by using fluorescence, circular dichroism (CD), Fourier transforms infrared (FTIR), three-dimensional (3D) fluorescence spectroscopy, and molecular docking techniques. The Stern–Volmer quenching constants KSV and the corresponding thermodynamic parameters ΔH, ΔG, and ΔS have been estimated by the fluorescence quenching method. The results indicated that parecoxib binds spontaneously with HSA through van der Waals forces and hydrogen bonds with binding constant of 3.45 × 104 M−1 at 298 K. It can be seen from far-UV CD spectra that the α-helical network of HSA is disrupted and its content decreases from 60.5% to 49.6% at drug:protein = 10:1. Protein tertiary structural alterations induced by parecoxib were also confirmed by FTIR and 3D fluorescence spectroscopy. The molecular docking study indicated that parecoxib is embedded into the hydrophobic pocket of HSA.