Drug-Biomacromolecule Interaction XII: Comparative binding study of sulfaethidole to bovine serum albumin by equilibrium dialysis, fluorescence probe technique, uv difference spectrophotometry and circular dichroism

1989 ◽  
Vol 12 (3) ◽  
pp. 160-165 ◽  
Author(s):  
Chong-Kook Kim ◽  
Yang-Sook Chun ◽  
Woon-Lyong Lah
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Fluorescence Probe ◽  
Equilibrium Dialysis ◽  
Binding Study ◽  
Probe Technique ◽  
Fluorescence Probe Technique ◽  
Comparative Binding ◽  
Circular Dichroïsm

scholarly journals 3-hydroxyflavone-bovine serum albumin interaction in Dextran medium

2015 ◽  
Vol 80 (4) ◽  
pp. 517-528 ◽  
Author(s):  
Mariana Voicescu ◽  
Sorana Ionescu
Keyword(s):  
Circular Dichroism ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Fluorescence Probe ◽  
Tryptophan Fluorescence ◽  
Intramolecular Proton Transfer ◽  
Biological Evaluation ◽  
Intrinsic Tryptophan Fluorescence ◽  
Circular Dichroïsm

Spectroscopic analysis of a bioactive flavonol, 3-Hydroxyflavone (3-HF), in systems based on Dextran 70 (Dx70) (an important bio-relevant polysacharide) and Bovine Serum Albumin (BSA) (a carrier protein), have been studied by fluorescence and circular dichroism. Changes produced by different concentrations of Dx70 on the fluorescent characteristics of 3-HF, and on the excited - state intramolecular proton transfer (ESIPT) process were studied. The influence of 3-HF binding and of Dx70 on the secondary structure of BSA were investigated by circular dichroism spectroscopy. The influence of temperature (30-80?C range) on the intrinsic Tryptophan fluorescence in 3-HF/BSA/Dx70 systems, was investigated. The results are discussed with relevance to 3-HF as a sensitive fluorescence probe for exploring flavone-protein interaction in plasma expander media and also for its biological evaluation.

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