Related Experiment Video
Updated: Jul 13, 2026

Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of Gold(III)
Published on: August 31, 2018
[Spectroscopic study on binding of indomethacin to bovine serum albumin]
1Center of Analysis and Test, Shanxi Normal University, Linfen 041004, China.
Abstract:
The interaction between indomethacin (IM) and bovine serum albumin (BSA) under physiological condition was studied using fluorescence and absorption spectra. It was proved that fluorescence quenching of BSA by IM is deduced by combining static quenching with nonradiative energy transfer. The binding constants were obtained by fluorescence quenching method. The main sorts of binding force were determined according to the thermodynamic parameters. The binding distances and energy transfer efficiencies between indomethacin and bovine serum albumin were obtained based on the theory of Forster nonradiative energy transfer. Combining the results of UV absorption and fluorescence spectroscopic methods, the binding mode of IM with BSA was discussed.
Related Concept Videos
Factors Affecting Protein-Drug Binding: Protein-Related Factors
The physicochemical properties of a drug play a significant role in its ability to bind to proteins. Lipophilic drugs, which dissolve in fats, oils, and lipids, can be bound by...
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...
Drug Binding to Blood Components
HSA is the most abundant plasma protein and is vital in drug binding. It contains distinct drug-binding sites, with different drugs exhibiting affinity for specific sites. There are three main drug-binding domains for HSA: sites I, II, and III. These domains are further...
Drug Distribution: Plasma Protein Binding
IR and UV–Vis Spectroscopy of Carboxylic Acids
However, the stretching absorptions for the C=O bond vary depending on the structure of carboxylic acids. The C=O bond of the free carboxylic acids shows a higher stretching frequency, 1760 cm−1, while H-bonded carboxylic acids (dimers) exhibit stretching absorptions at a lower frequency, 1710 cm−1. The C=O bond of the...
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,...

