Fluorescence quenching and ligand binding: A critical discussion of a popular methodology

Study of the interaction of an anticancer drug with human and bovine serum albumin: Spectroscopic approach

Studies of interaction between colchicine and bovine serum albumin by fluorescence quenching method

Interaction of the flavonoid hesperidin with bovine serum albumin: A fluorescence quenching study

In this paper, the interaction between p-aminoazobenzene (PAAB) and BSA was investigated mainly by fluorescence quenching spectra, circular dichroism (CD) and three-dimensional fluorescence spectra under simulative physiological conditions. It was proved that the fluorescence quenching of BSA by PAAB was mainly a result of the formation of a PAAB-BSA complex. The modified Stern-Volmer quenching constant Ka and the corresponding thermodynamic parameters ΔH, ΔG and ΔS at different temperatures were calculated. The results indicated that van der Waals interactions and hydrogen bonds were the predominant intermolecular forces in stabilizing the complex. The distance r = 4.33 nm between the donor (BSA) and acceptor (PAAB) was obtained according to Forster’s non-radioactive energy transfer theory. The synchronous fluorescence, CD and three-dimensional fluorescence spectral results showed that the hydrophobicity of amino acid residues increased and the losing of α-helix content (from 63.57 to 51.83%) in the presence of PAAB. These revealed that the microenvironment and conformation of BSA were changed in the binding reaction.

Fluorescence Study on the Interaction of Bovine Serum Albumin with P-Aminoazobenzene

Study of the interaction between monoammonium glycyrrhizinate and bovine serum albumin

The interaction between methylene blue (MB) and bovine serum albumin (BSA) was investigated by fluorescence and UV–vis absorbance spectroscopy. In the mechanism discussion, it was proved that the fluorescence quenching of BSA by MB is mainly a result of the formation of MB–BSA complex and electrostatic interactions play an important role to stabilize the complex. The Stern–Volmer quenching constant K SV and corresponding thermodynamic parameters Δ H , Δ G , and Δ S were calculated. The distance r between donor (BSA) and acceptor (MB) was obtained according to fluorescence resonance energy transfer (FRET). The effect of MB on the conformation of BSA has been analyzed by means of UV–vis absorbance spectra and synchronous fluorescence spectroscopy.

Song-Sheng Qu

Papers

Study of the interaction between monoammonium glycyrrhizinate and bovine serum albumin

Studies of interaction between colchicine and bovine serum albumin by fluorescence quenching method

Spectroscopic studies on the interaction between methylene blue and bovine serum albumin

Studies on the interaction between 1-hexylcarbamoyl-5-fluorouracil and bovine serum albumin

Interaction of cromolyn sodium with human serum albumin: a fluorescence quenching study.