Interaction between malachite green and bovine serum albumin

The interaction between malachite green (MG) and bovine serum albumin (BSA) was investigated via fluorescence and ultraviolet-visible absorption spectra in buffer solutions at different temperatures. The experimental results showed that static quenching was involved in adding MG in BSA solution. The binding constants (K-A) were 7.69x 10(4)L.mol(-1)(10 degrees C), 5.31 x 10(4) L.mol(-1)(20 degrees C), and 4.85 x 10(4) L.mol(-1) (37 degrees C), respectively, and they reacted at a molar ratio of 1:1. The energy transfer efficiency E was 0.1635 and the binding distance r was 2.30 nm between MG and BSA according to Forster non-radiative energy transfer mechanism. The interaction between MG and BSA was driven mainly by hydrogen bonds and Vander Waals force according to thermodynamic parameters.