Abstract

Comparative studies on the interaction of tartrazine with bovine serum albumin by fluorescence quenching spectroscopy and synchronous fluorescence spectroscopy

Author(s): Lihui Zhang, Baosheng Liu, Zhiyun Li, Ying Guo, Yunkai Lv

Under simulated physiological conditions, the reactionmechanismbetween tartrazine (TTZ) and bovine serumalbumin (BSA) at different temperatures (293 K, 303 K, 310 K)was investigated by fluorescence quenchingmethod and synchronous fluorescence method, respectively. The results indicated that the fluorescence intensity and synchronous fluorescence intensity of BSA decreased regularly with the addition of TTZ, in addition, the quenching mechanism, binding constants (Ka), the number of binding site (n), type of interaction force and energy transfer parameters of TTZ with BSA obtained from two methods by the same equation were consistent, which indicated synchronous fluorescence spectrometrywas a newmethod of studying the binding mechanism between drug and protein, and it was a useful supplement to the classical method.