Synthesis And Basic Studies Of Two Schiff Bases Compounds

The article analysed the harm to human caused by environment pollution, and studied two Schiffbases compounds interacted with the bovine serum albumin (BSA) under physiological pH conditions. TheUV-Visible absorption spectroscopy combined with fluorescence spectroscopy were employed to investigateon study the quenching mechanism of BSA,thermodynamic binding parameters，the type of binding force,the binding sites number and binding constant，and the effect of two Schiff base small molecules on theconformation of BSA, etc, which had a certain significance of pharmaceutical science and clinical medicine.The present work consists of the following several parts:1. Synthesis of two Schiff base compounds and characterized by FTIR、MS、1HNMR.2. The fluorescence quenching method and UV-visible spectrometry were employed to investedon studying the interactions between the bovine serum albumin (BSA) and two Schiff base compounds forthe reason that some small molecules lead the intrinsic fluorescence of bovine serum albumin quenching.Combining with the Stern-Volmer equation, we determined the quenching process were static quenching.Based on double logarithmic equation, we calculated the binding constants of the two Schiff base compoundswith bovine serum albumin and the corresponding number of binding sites at different temperatures.According to thermodynamic parameters of equations, we calculated he corresponding ΔH, ΔS and ΔGvalues and inferred that the type of force between the bovine serum albumin (BSA) and two Schiff basecompounds were hydrogen bonds and van der Waals force. According to the F rster non-radiative energytransfer theory, we calculate the binding distance between the two Schiff base compounds with bovine serumalbumin. 3. The synchronous fluorescence and UV-Visible absorption spectroscopy were employed toinvested on studying the conformational change of bovine serum albumin (BSA) leaded by the Schiff basecompounds. The results showed that two Schiff base compounds did not cause a conformational change ofbovine serum albumin(BSA).