Study On The Interaction Between Four Classes Of Nitrogenous Heterocyclic Compounds And Bovine Serum Albumin Via Flourensence Spectroscopy

Serum albumin is the important carrier and target molecule, which has many essential functions, such as material storage, transport, distribution and metabolism process. In recent years, small molecules with serum albumin interaction studies have been a hot pot of concern. Study of the interaction between small molecular and SA at the molecular level is of particular value in metabolism, new drug design, pharmacokinetics, and clinical medication safety. In this dissertation, In order to study the interaction of four nitrogenous heterocyclic compounds and bovine serum albumin (BSA), the fluorescence and UV-vis spectroscopy were used. The dissertation includes four parts.1. The spectrum technologies were explored to study the interaction mechanism between edaravone (EDA) and bovine serum albumin (BSA). The results revealed that EDA had a quite strong ability, which could lead to the fluorescence of BSA decrease. We also calculated the binding constants, number of binding sites and binding distances. Furthermore, In order to study the effect of EDA on the conformation of BSA, the synchronous fluorescence spectra were employed. What’s more, the effects of four common metal ions on the binding constant between EDA and BSA were examined.2. The interaction between imidazo[2,1-b]thiazole (IMTZ) and bovine serum albumin (BSA) was analyzed by fluorescence and ultraviolet spectroscopy. The experimental results showed that the quenching mechanism is combined quenching process in different temperatures. Comparision the binding constants of IMTZ five compounds with BSA binding constants, it could enhanced the binding affinity when the substituting groups exsist on benzene ring. According to the non-radiation energy transfer theory, we calculated the binding distances of IMTZ-BSA.3. Using the fluorescence quenching theory we obtained the combined quenching is the quenching mechanism between TZPM and BSA. To explore the effect of molecular structure on the binding, we obtained quantum chemical parameters and structural parameters (the highest occupied orbital energy (EH), the lowest occupied orbital energy (EL), the dipole moment (μ), Molar Volume (Vm) and so on), and a study on quantitative structure-property relationship (QSPR) was performed, the quantitative relationship equation of R0, r and Ka were obtained. Furthermore, we investigated the possible sub-domains on BSA that bind TZPM by displacement experiments.4. We studied the interaction of lomefloxacin (LOM) and bovine serum albumin (BSA) in the Britton-Robinson buffer with four different pHs. The datas showed that BSA had reacted with LOM, meanwhile, formed a new compound. The distances between BSA and LOM were less than7nm. The pH can affect the binding between LOM and BSA and LOM has the optimal condition of binding constant and binding distance at pH4.9. Synchronous fluorescence spectrometry indicated that LOM has a remarkable influence on the conformation of BSA in different pHs.