Electrochemical And Spectral Study On The Interaction Between Drugs And Bovine Serum Albumin

Protein is an essential material of organisms, it plays an important role in life activities. The establishment of drug-protein binding model in vitro, understanding of binding tightness, binding sites, binding force and binding constant contribute to cognitive the interaction mechanism and rule, which will provide available information and data in the life science research.In this thesis, the interaction of 3,3',3",3"'-ethylenetetrakis-4-hydroxycoumarin (EHC) with bovine serum albumin (BSA) was studied detailedly by UV-vis absorption, fluorescence spectrometry and electrochemical technique. Besides, the direct electrochemical behavior of both hemoglobin (Hb) and myoglobin (Mb), as well as their electrocatalysis to the reduction of hydrogen peroxide were investigated by means of a variety of electrochemical methods. In addition, the interaction of Hb with (3,4)-bis-(4-hydroxyl-3-coumarin)-2,5-hexylene glycol (HCH) was investigated by differential pulse voltammetry and amperometry. These studies will play the important role in the development of anti-AIDS drugs and understanding of the nature of life processes.This thesis consists of five chapters and the main contents are summarized as follows:1. The interaction of 3,3',3",3'"-ethylenetetrakis-4-hydroxycoumarin (EHC) with bovine serum albumin (BSA) was studied by UV-vis absorption spectrometry and fluorescence spectrometry both in acetate (pH 4.70) and phosphate (pH 7.40) buffer solutions, then the effect of EHC on the conformation of BSA was investigated by UV-vis absorption spectrometry. The binding ration and binding constant were calculated. The interaction forces at different pHs were elucidated according to the thermody parameters, the binding site of EHC in BSA was concluded. Lastly the effect of BSA on the electrochemical reduction behavior of EHC was discussed by electrochemical method.2. Myoglobin (Mb) was immobilized into the cellulose diacetate/ 1-butyl-3-methyl-imidazolium tetrafluoroborate (CDA-[bmim]BF4) film by the simple casting method, and Mb was characterized by UV-vis spectroscopy and electrochemical impedance spectroscopy. The direct electron transfer of Mb on the modified glassy carbon electrode and electrocatalysis of Mb towards H2O2 were investigated, based on which the hydrogen peroxide biosensor was constructed. This study provided an efficient matrix for the immobilization of redox protein and development of electrochemical biosensors.3. The direct electron transfer of hemoglobin (Hb) immobilized in biocompatible chitosan (Chi) and ionic liquid 1-butyl-3-methyl-imidazolium tetrafluoroborate ([bmim]BF4) on the modified glassy carbon electrode was investigated, which realized electrocatalysis of Hb towards H2O2. The interaction of Hb with the inhibitor of HIV-1 protease and integrase (3,4)-bis-(4-hydroxyl-3-coumarin)-2,5-hexylene glycol (HCH) was investigated by differential pulse voltammetry and amperometry which was a novel method in the field of binding studies. The biosensor exhibited an attractive ability to measure H2O2 or HCH.