Interaction between 1-Hydroxypyrene with Bovine Serum Albumin

Mechanism of the interaction between 1-hydroxypyrene (1-HP) and bovine serum albumin (BSA) was studied by fluorospectrometry and UV-VIS spectrophotometry. It was found that significant quenching of fluorescence of BSA appeared by its reaction with 1-HP. As judged from the fluorescence quenching constants obtained by Stern-Volmer equation, fluorescence quenching of BSA by 1-HP was attributed to static quenching. The binding constant, number of binding sites and binding distance were found by applying the equation of site-binding model and Frster′s nonradiative energy transfer theory. Values of thermodynamic parameters ΔH and ΔS were calculated and based on these results, the binding force of the reaction was due to hydrogen bond and Vander Waals force.