Interaction and Molecular Simulation between Gossypol and Human Serum Albumin
- VernacularTitle:棉酚与人血清白蛋白相互作用及其分子模拟研究
- Author:
Jian YANG
;
Jurong LI
;
Xianxi GUO
;
Zhifeng DU
;
Fang ZHANG
- Publication Type:Journal Article
- Keywords:
Gossypol;
Human serum albumin;
Fluorescence quenching;
Molecular simulation
- From:
China Pharmacist
2015;(6):881-883,887
- CountryChina
- Language:Chinese
-
Abstract:
Objective:To explore the interaction between gossypol and human serum albumin ( HSA) . Methods:The interaction of gossypol and HSA under physiological conditions was studied by fluorescence spectroscopy, and the molecular docking software was used to simulate the interaction. Results:The binding constant of gossypol and HSA at 293K and 303K was 2. 390 6 × 105 L·mol-1 and 3. 576 8 × 103 L·mol-1 , respectively. There was one binding site on HSA for gossypol. Hydrogen bond and Van Der Waals inter-actions were involved in the binding process. The binding of gossypol and HAS was closer to tyrosine residue in HSA. The molecular simulation analysis verified the above results. Conclusion: The gossypol-induced fluorescence quenching of HSA belongs to a static quenching procedure.
