Abstrait

Study on the interaction between bilirubin and human serum albumin by fluorescence spectroscopy

Ling Li, GongWu Song, Juan Chen, Cheng Fang Li

The interactions between bilirubin and human serum albumin (HSA) have been studied by fluorescence spectroscopy. The fluorescence quenching spectrum was studied at different temperature by Stern-Volmer and Lineweaver-Burk equations. The main binding force of bilirubin to HSA was judged according to the thermodynamic parameters. The binding distance between bilirubin and protein was also obtained. Furthermore, the binding constant was measured by fluorescence quenching and enhancement spectrum, respectively. The observed spectral results revealed that there were strong interactions between bilirubin and protein, the mechanism of quenching belonged to static quenching and the main binding force was van der Waals interactions and hydrogen bonds.