Comparative Studies on the Interaction of Aspirin with Bovine Serum Albumin by Fluorescence Quenching Spectroscopy and Synchronous Fluorescence Spectroscopy

2015 ◽  
Vol 48 (6) ◽  
pp. 441-446 ◽  
Author(s):  
Li-Hui Zhang ◽  
Bao-Sheng Liu ◽  
Zhi-Yun Li ◽  
Ying Guo
Keyword(s):  
Bovine Serum Albumin ◽  
Fluorescence Quenching ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Comparative Studies ◽  
Bovine Serum ◽  
Synchronous Fluorescence ◽  
Synchronous Fluorescence Spectroscopy

The Investigation of the Interaction between Daidzin and Bovine Serum Albumin by Fluorescence Spectroscopy

2014 ◽  
Vol 664 ◽  
pp. 402-409
Author(s):  
Qing Ming Wang ◽  
Jia Liu ◽  
Tian Xing Zhang ◽  
Feng Zhu ◽  
Xin Hui Tang
Keyword(s):  
Bovine Serum Albumin ◽  
Hydrogen Bonds ◽  
Fluorescence Quenching ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Binding Constant ◽  
Bovine Serum ◽  
Hydrophobic Interactions ◽  
Binding Constants ◽  
Apparent Binding Constant

We investigated the mutual interaction of daidzin with bovine serum albumin (BSA) by fluorescence spectroscopy. The results revealed that daidzin cause the fluorescence quenching of BSA through a static quenching procedure. The Stern-Volmer quenching constant (Ksv) were calculated at different temperature. The binding site (n), apparent binding constant (Ka) and corresponding thermodynamic parameters △Go, △Ho, △Sowere calculated and the van der Waals interaction, hydrogen bonds and hydrophobic interactions play an important role in stabilizing the complex. Besides, we also studied the effect of Cu2+, Ni2+, Mn2+and Co2+on the binding constants between daidzin and BSA, it is shows that the binding of BSA and daidzin is strengthened in the presence metal ions.

Sign in / Sign up

Export Citation Format

Share Document