| Some functional groups of biopolymers can bind with the molecular of drugs, which afford biopolymer complexes. These biopolymer complexes keep the physiological activities of biopolymer, along with decreasing the toxicity and allergies of drugs. As most of low-molecular-weight drugs showed some disadvantages. For example, the blood concentration of drug treatment is too high in a short time after delivery, and sometimes even higher than minimum concentration of poisoning, causing human cases of allergies, poisoning. Therefore, binding to biopolymers is a kind of good ways to overcome their disadvantages of low-molecular-weight drugs.Albumin is a kind of important transport carriers for drugs. The binding of drugs with protein has a great influence not only upon the distribution of the drugs in the body but also upon their patterns of metabolism and excretion. Thus, the study of the binding characteristics of small-molecular-weight drug to albumin is an important topic in nature polymer and medical researcher. The dissertation consists of four chapters:Chapter 1: The developments of interaction of drugs with protein were reviewed. Some methods used to study the interaction of drugs with protein were summarized.Chapter 2: The binding pazufloxacin mesylate with bovine serum albumin was investigated by the fluorescence and UV-Vis spectra. It indicated that pazufloxacin mesylate can bind to bovine serum albumin and pazufloxacin mesylate can quench the fluorescence of bovine serum albumin. The dominant sorts of binding forces are mainly electrostatic and hydrophobic force.Chapter 3: The binding of cefpiramide to bovine serum albumin was studied by the fluorescence spectra and the native polyacrylamide gel electrophoretic (PAGE). The results showed that cefpiramide can strongly bind to bovine serum albumin. The binding constant is KA=6.157×104 L·mol-1 and the number of binding, n=1 at 299K. and native PAGE revealed that the structure of the BSA was kept after binding cefpiramide.Chapter 4: The fluorescence quenching reactions of ceftazidime with bovine serum albumin in solution were studied. The quenching mechanism of bovine serum albumin by ceftazidime was interpreted using Stern-Volmer (S-V) mechanism. The binding constant K values were calculated. In addition, the thermodynamic functions enthaipy and entropy for reaction were also calculated according to Vant's Hoff equation. FT-IR spectra were used to investigate the changes of bovine serum albumin structure after interaction of ceftazidime with bovine serum albumin. |
PDF Full Text Request