Related Experiment Video
Updated: Nov 21, 2025

Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps
Published on: July 19, 2024
Delineating the interaction mechanism of glabridin and ovalbumin by spectroscopic and molecular docking techniques
Md Abdur Razzak1, Shin Sik Choi2
1Department of Energy Science and Technology, Myongji University, Yongin 17058, Republic of Korea.
Abstract:
The interaction between ovalbumin (OVA) and isoflavonoid glabridin (GB) was investigated using spectroscopic and molecular docking techniques. Fluorescence spectroscopy revealed that GB was bound to OVA mainly due to hydrogen bonding and hydrophobic forces. FT-IR spectroscopy showed that the combination of GB and OVA resulted in a decrease in the β-sheet content of OVA and an increase in the α-helix and extended-chain content. All these experimental results were supported and clarified by molecular docking simulations. GB binding was able to inhibit chemical denaturant-induced structural changes in OVA as observed by intrinsic tryptophan and ANS fluorescence. Moreover, GB-OVA complex increased the aqueous solubility of GB by about 4.45 times at pH 7.0. These results provided insights into the interaction between GB and OVA that contributes to the utilization of GB in the food and pharmaceutical industries.
More Related Videos
08:49Incorporating Target Protein Structure Flexibility and Dynamics in Computational Drug Discovery Using Ensemble-Based Docking Analysis
Published on: June 20, 2025
08:58Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
Published on: July 5, 2018
Related Concept Videos
The Equilibrium Binding Constant and Binding Strength
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,...
Ligand Binding Sites
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Protein-Drug Binding: Determination Methods
Indirect methods involve isolating the bound drug from its free form in biological samples such as blood, serum, or plasma. These techniques aim to measure the percentage of drugs bound to proteins. Equilibrium dialysis is a commonly used method where the free drug concentration at equilibrium is measured by separating the bound...
Ligand Binding and Linkage
Globular and Fibrous Proteins
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...