The investigation of the interaction between NCP–EDA and bovine serum albumin by spectroscopic approaches

Abstract

The fluorescence and ultraviolet spectroscopies were explored to study the interaction between N-confused porphyrins–edaravone diad (NCP–EDA) and bovine serum albumin (BSA) under simulative physiological condition at different temperatures. The experimental results show that the fluorescence quenching mechanism between NCP–EDA and BSA is a combined quenching (dynamic and static quenching). The binding constants, binding sites and the corresponding thermodynamic parameters (Δ G, Δ H, and Δ S) of the interaction system were calculated at different temperatures. According to Förster non-radiation energy transfer theory, the binding distance between NCP–EDA and BSA was calculated to be 3.63 nm. In addition, the effect of NCP–EDA on the conformation of BSA was analyzed using synchronous fluorescence spectroscopy.