Interaction of magnolol with HSA/BSA and analysis of the feasibility of modeling equation
10.11669/cpj.2013.24.005
- Author:
Ming GUO
1
Author Information
1. School of Engineering
- Publication Type:Journal Article
- Keywords:
Equation modelin;
Magnolol;
Molecular modeling;
Serum albumin;
Spectrum experiment
- From:
Chinese Pharmaceutical Journal
2013;48(24):2089-2097
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVE: To investigate the reaction mechanisms of magnolol (MG) binding with bovine serum albumin (BSA) and human serum albumin(HSA) by using different equations. METHODS: The characteristic spectra of HSA/BSA-MG interaction system were determined by using spectral experiment. The binding constants, energy transfer parameters and thermodynamic parameters were calculated by logarithmic equation and nonlinear equation, and the influence of MG on molecular conformation of BSA/HSA was also investigated. A comparative analysis of the interaction of MG with HSA/BSA was performed. The different equations were applied to deal with the experimental data and the feasible modeling equation was suggested. RESULTS: Static quenching exited between MG and SA with significant bond strength. The value of binding distances (r) was low, which indicated the occurrence of energy transfer. Fluorescent phase diagram technical analysis showed that the reaction conformational pattern of MG-BSA was "two-state" model; MG-HSA was a sequence change process. According to the obtained thermodynamic parameters, the main interactional forces between MG and SA were judged to be hydrogen bonds and Van der Waals forces. The results of molecular modeling revealed that hydrogen bonds and Van der Waals forces were the main binding forces in the MG-BSA/HSA system, and hydrophobic interaction was also present. These results were in accordance with spectral experiments. CONCLUSION: There are differences between the interaction mechanisms of MG-BSA and MG-HSA. Logarithmic equation is the most suitable equation for this system.
