- Journal of the Turkish Chemical Society Section A: Chemistry
- Volume:7 Issue:3
- Investigation of Triamcinolone-Bovine Serum Albumin (BSA) Interaction by Spectroscopic Methods
Investigation of Triamcinolone-Bovine Serum Albumin (BSA) Interaction by Spectroscopic Methods
Authors : Sabriye AYDINOĞLU
Pages : 903-910
Doi:10.18596/jotcsa.782263
View : 49 | Download : 9
Publication Date : 2020-10-30
Article Type : Research Paper
Abstract :The aim of the present study was investigate the interaction between bovine serum albumin and triamcinolone. For this purpose, the interaction between BSA and triamcinolone was evaluated by UV–Vis and fluorescence spectroscopy under different temperatures, and different salt concentration at physiological pH insert ignore into journalissuearticles values(7.4);. The binding constant of BSA-Triamcinolone system were evaluated different temperature at constant insert ignore into journalissuearticles values(pH =7.4); and ionic strength insert ignore into journalissuearticles values(0.01 M);. The binding constant dependence of binding constant on temperature was analysed by Van’t Hoff equation. The standard enthalpy change insert ignore into journalissuearticles values(DeltaH); and standard entropy change insert ignore into journalissuearticles values(DeltaS); values were determinated respectively as 9.0 kcal/mol while as 54.1 cal/mol.K.. In addition, the effect of salt concentration investigated for BSA-Triamcinolone system at constant temperature insert ignore into journalissuearticles values(T=25°C); and increasing salt concentration lead to decrement on the binding constant value. The obtained thermodynamic parameters indicate hydrophobic forces take major role in BSA-Triamcinolone interaction. The arousal of salt concentration prompted to diminution on affinity between Triamcinolone and BSA.Keywords : Triamcinolone, Bovine Serul Albumin, Drug Protein Interaction, Thermodynamics, Spectroscopy
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