Investigation of Triamcinolone-Bovine Serum Albumin (BSA) Interaction by Spectroscopic Methods

Abstract

The aim of the present study was investigate the interaction between bovine serum albuminand triamcinolone. For this purpose, the interaction between BSA and triamcinolone was evaluated byUV–Vis and fluorescence spectroscopy under different temperatures and different salt concentrations atphysiological pH (7.4). The binding constant of BSA-Triamcinolone system were evaluated differenttemperature at constant (pH=7.4) and ionic strength (0.01 M). The binding constant dependence ofbinding constant on temperature was analyzed by Van’t Hoff equation. The standard enthalpy change(ΔH) was 9.0 kcal/mol and standard entropy change (ΔS) was 54.1 cal/mol K. In addition, the effect ofsalt concentration investigated for BSA-Triamcinolone system at constant temperature (T=25 °C) andincreasing salt concentration lead to decrement on the binding constant value. The obtainedthermodynamic 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.