Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
7593377 | Food Chemistry | 2015 | 7 Pages |
Abstract
Overconsumption of erucic acid has been shown to cause heart damage in animals. The aim of this study is to evaluate the binding behaviour between erucic acid and bovine serum albumin using multi-spectroscopic methods and a molecular docking technique under physiological conditions. We find that erucic acid can quench the intrinsic fluorescence of BSA by dynamic quenching and there is a single class of binding site on BSA. In addition, the thermodynamic functions ÎH and ÎS are 119.14 kJ molâ1 and 488.89 J molâ1 Kâ1, indicating that the hydrophobic force is a main acting force. Furthermore, the protein secondary structure changes with an increase in the content of α-helix, measured using synchronous fluorescence, circular dichroism and Fourier transform infrared spectroscopies. The molecular docking results illustrate that erucic acid can bind with the subdomain IIA of the BSA, and hydrogen bonding is also an acting force.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Yang Shu, Weiwei Xue, Xiaoying Xu, Zhimin Jia, Xiaojun Yao, Shuwen Liu, Lihong Liu,