Analysis on molecular interaction mechanism of verbascoside binding with serum albumin by spectroscopy and molecular modeling method
10.7501/j.issn.0253-2670.2015.04.015
- Author:
Ming GUO
1
Author Information
1. School of Science, Zhejiang Agricultural & Forestry University
- Publication Type:Journal Article
- Keywords:
Binding reaction;
Bovine serum albumin;
Molecular modeling;
Spectrum experiment;
Verbascoside
- From:
Chinese Traditional and Herbal Drugs
2015;46(4):541-548
- CountryChina
- Language:Chinese
-
Abstract:
Objective: To study the molecular mechanism of the binding reaction between verbascoside (VER) and bovine serum albumin (BSA). Methods: Under physiological conditions, the interaction parameter of drug binding with protein was determinated by spectroscopy, VER-BSA interactional model was built and the binding reaction mechanism was analyzed. Results: The established VER-BSA binding model suggested that VER can strongly bind to BSA mainly by hydrogen bonds interaction and Van der Waals force, there were hydrophobic interactions, too. The results from spectroscopy indicated that static quenching exited between VER and BSA with significant strong bond. The value of binding distances (r) was low, which indicated the occurrence of energy transfer. Through fluorescent phase diagram technical analysis, the reaction conformational pattern of VER-BSA showed "two-state" model. According to the obtained thermodynamic parameters, the main interactional force between VER and BSA was hydrogen bonds interaction and Van der Waals force. The fluorescence polarization proved that VER and BSA generated a non-covalent complex. Conclusion: The experiment results are agreed with the molecular modeling, which provides the helpful reference for the study on molecular reaction mechanism of VER binding with BSA.
