Molecular spectroscopic studies on the interaction of morin with bovine serum albumin
- 作者：Yan-Jun Hu ; huyj@whu.edu.cn ; yjhu@263.net ; Hua-Li Yue ; Xiao-Ling Li ; Si-Si Zhang ; E. Tang ; Li-Ping Zhang
- 关键词：Morin ; Bovine serum albumin ; Conformational investigation ; Binding parameters ; Structure&ndash ; affinity relationship
- 刊名：Journal of Photochemistry and Photobiology B ; Biology
- 出版年：2012
- 期刊代码：67_10111344
- 类别：ch
- 出版时间：2 July, 2012
- 卷：112
- 期：Complete
- 页码：16-22
- 文件大小：474 K
摘要
The interaction between morin and bovine serum albumin (BSA) was studied using molecular spectroscopic approach at different temperatures under imitated physiological conditions. Quenching of intrinsic tryptophanyl fluorescence of BSA with increasing morin concentration is the actuating tool in the analysis. The obtained quenching mechanisms, binding constants, binding sites and corresponding thermodynamic parameters at different temperatures indicate that the hydrophobic interaction play a major role in the morin-BSA association. Binding affinity between morin and BSA was determined using Scatchard equation and the modified Stern-Volmer equation, and the corresponding Structure-affinity relationships of flavonoids were discussed. Site marker competitive displacement experiments demonstrated that morin binds with high affinity to site II (subdomain IIIA) of BSA. Furthermore, the circular dichroism spectral results indicated that the conformation of BSA changed in the presence of morin. In addition, the effect of some common metal ions on the binding constant between morin and BSA was examined.