Related Experiment Video
Updated: May 17, 2026

Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of Gold(III)
Published on: August 31, 2018
Insight into the dynamic interaction between different flavonoids and bovine serum albumin using molecular dynamics
Xiaodi Niu1, Xiaohan Gao, Hongsu Wang
1Department of Food quality and Safety, Jilin University, Changchun 130062, People's Republic of China. niuxd@jlu.edu.cn
Abstract:
In this study, the binding of Bovine serum albumin (BSA) with three flavonoids, kaempferol-3-O-a-L-rhamnopyranosyl-(1-3)-a-L-rhamnopyranosyl-(1-6)-b-D-galacto- pyranoside (drug 1),kaempfol-7-O-rhamnosyl-3-O-rutinoside (drug 2)andkaempferide-7-O-(4"-O-acetylrhamnosyl)-3-O-ruti- noside (drug 3) is investigated by molecular docking, molecular dynamics (MD) simulation, and binding free energy calculation. The free energies are consistent with available experimental results and suggest that the binding site of BSA-drug1 is more stable than those of BSA-drug2 and BSA-drug3. The energy decomposition analysis is performed and reveals that the electrostatic interactions play an important role in the stabilization of the binding site of BSA-drug1 while the van der Waals interactions contribute largely to stabilization of the binding site of BSA-drug2 and BSA-drug3. The key residues stabilizing the binding sites of BSA-drug1, BSA-drug2 and BSA-drug3 are identified based on the residue decomposition analysis.
More Related Videos
Related Concept Videos
Protein-Drug Binding: Mechanism and Kinetics
Various forces drive these interactions, including hydrogen bonds, hydrophobic interactions, ionic bonds, electrostatic interactions, and van der Waals forces. These bonds enable drugs to bind to specific sites on proteins,...
The Equilibrium Binding Constant and Binding Strength
The Equilibrium Binding Constant and Binding Strength
Measurement of Bioavailability: Pharmacodynamic Methods
Nonlinear Pharmacokinetics: Bioavailability and Protein-Drug Binding
To quantify the extent of bioavailability, pharmacologists often use a parameter called .
Physiological Pharmacokinetic Models: Assumption with Protein Binding

