Spectroscopic analysis on the binding interaction of biologically active pyrimidine derivative with bovine serum albumin

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.

Three-dimensional chitin rings from body segments of a pet diplopod species: Characterization and protein interaction studies

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Ferrocene‐substituted bis(ethynyl)anthracene compounds as anticancer agents

“…The blue shift indicates that, after the addition of the compounds, the polarity around the fluorescence chromophore (such as tryptophan, tyrosine) of BSA decreases due to which the hydrophobicity increases and the peptide strands become less extended. The result suggests that the conformation of the protein slightly changes . At 340 nm, the intensity of the fluorescence spectral band is quenched up to 40% of its initial value (Figure ).…”

Photophysical Characterization and BSA Interaction of Direct Ring Carboxy Functionalized Symmetrical squaraine Dyes

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