Interaction of the Testosterone with Bovine Serum Albumin (BSA): UV-Visible Absorption Spectroscopy
Abu Sharkh, Sawsan
Abu Teir, Musa
The molecular interactions between BSA and Testosterone have been successfully investigated. The absorption, distribution and metabolism of many molecules can be altered based on their affinity to BSA. BSA is often increases the apparent solubility of hydrophobic ligands in plasma and modulate their delivery to cells. In this study, the interaction between Testosterone and BSA has been investigated using UV- absorption spectrophotometry and fluorescence spectroscopy to determine the binding constant. From UV- absorption spectrophotometry which showed a decreasing in the absorption intensity with increasing of the molecular ratios of testosterone to BSA, it is found that the value of the binding constant of testosterone to BSA, K equals 0.415*103 M-1 at 293 K. While from the Fluorescence spectroscopy there was a quenching in the intensity with increasing of the molecular ratios of testosterone to BSA and it gave the same value of the binding constant as uv-absorption spectroscopy.
Testosterone , Bovine Serum Albumin , binding mode , binding constant , UV–spectroscopy , Fluorescence spectroscopy