Related Experiment Video
Updated: Feb 14, 2026

Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of GoldIII
Published on: August 31, 2018
Spectroscopic analysis on the binding interaction of biologically active pyrimidine derivative with bovine serum
Vishwas D Suryawanshi1, Laxman S Walekar1, Anil H Gore1
1Fluorescence Spectroscopy Research Laboratory, Department of Chemistry, Shivaji University, Kolhapur 416 004, Maharashtra, India.
Abstract:
A biologically active antibacterial reagent, 2-amino-6-hydroxy-4-(4-N, N-dimethylaminophenyl)-pyrimidine-5-carbonitrile (AHDMAPPC), was synthesized. It was employed to investigate the binding interaction with the bovine serum albumin (BSA) in detail using different spectroscopic methods. It exhibited antibacterial activity against Escherichia coli and Staphylococcus aureus which are common food poisoning bacteria. The experimental results showed that the fluorescence quenching of model carrier protein BSA by AHDMAPPC was due to static quenching. The site binding constants and number of binding sites (n≈1) were determined at three different temperatures based on fluorescence quenching results. The thermodynamic parameters, enthalpy change (ΔH), free energy (ΔG) and entropy change (ΔS) for the reaction were calculated to be 15.15 kJ/mol, -36.11 kJ/mol and 51.26 J/mol K according to van't Hoff equation, respectively. The results indicated that the reaction was an endothermic and spontaneous process, and hydrophobic interactions played a major role in the binding between drug and BSA. The distance between donor and acceptor is 2.79 nm according to Förster's theory. The alterations of the BSA secondary structure in the presence of AHDMAPPC were confirmed by UV-visible, synchronous fluorescence, circular dichroism (CD) and three-dimensional fluorescence spectra. All these results indicated that AHDMAPPC can bind to BSA and be effectively transported and eliminated in the body. It can be a useful guideline for further drug design.
Related Concept Videos
Ligand Binding and Linkage
The Equilibrium Binding Constant and Binding Strength
tRNA Activation
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...
Factors Affecting Protein-Drug Binding: Drug Interactions
Displacement interactions can have varying outcomes, ranging from toxicity to virtually...
Conserved Binding Sites
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...

