Study on the Interaction between Pantoprazole Sodium and Bovine Serum Albumin by Spectrometry

Under the optimal conditions，the interaction of Pantoprazole Sodium(PS) with bovine serum albumin(BSA) was investigated by fluorescence spectrometry and ultraviolet-visible light absorption spectrometry. It showed that the fluorescence of BSA was quenched by PS, which was a static quenching process. BSA could transport PS. It was spontaneous and mainly driven by hydrogen bond and Vander Waals force. The primary binding site for PS was located at sub-domain ⅡA of BSA and near by tyrosine residue. There was some positive cooperative effect. The conjugation reaction would affect the conformation of BSA, leading to the polarity around BSA weakened. This test provided a theoretical basis for revealing the pharmacokinetics and further research on development of new antibacterial drugs．