Font Size: a A A

Study On The Interaction Between Drugs And Bovine Serum Albumin

Posted on:2007-04-30Degree:MasterType:Thesis
Country:ChinaCandidate:C X XueFull Text:PDF
GTID:2144360212498159Subject:Applied Chemistry
Abstract/Summary:PDF Full Text Request
Serum albumins are the major soluble protein constituents, which are also the most plentiful depot and transport protein in blood plasma. Many endogenous compounds in human body and medicines can bind to them to form stable protein-medicine complexes with certain particular structures, which implement the function of regulating proteins directly or directly. The study of the interaction between small organic molecules especially drugs and serum albumin is distinctively important in pharmacology and pharmacokinetics because drug-protein binding affects the pharmacological activities and the drug absorption, distribution and elimination.In this thesis, the interactions of four kinds of antibiotics, four kinds of flavonoids with BSA were investigated by UV absorption and fluorescence spectroscopy methods. The interactions of clarithomyci, atorvastatin calcium with BSA were studied using electrochemical techniques. These studies would supply available informations and datas in life sciences.This thesis consists of five chapters, and the main contents are as follows:1. The interactions of Clindamycin, Roxithromycin, Kalamycin, and Cefdinir with BSA were studied by UV absorption spectra in pH7.17 phosphate buffer solution, respectively. The binding constant was obtained and the binding mechanism was discussed, primarily.2. The interactions of quercetin (QUE), daidzein (DAI), 4',7- dimethoxy -3' -isoflavone sulfonic sodium (DISS), and 3'-daidzein sulfonic sodium (DSS) with BSA were investigated using UV absorption and fluorescence spectroscopic methods. The interactional rules of protein-medicine were researched from the molecule configuration.3. The interaction between clarithomycin and BSA was investigated by linear-sweep voltammetry at mercury electrode in pH4.5~8.0 phosphate buffer solution. Over the studied pH range, three reduction waves of CAM which P1, P2 and P3 were produced. The electrode processes of AC and AC-BSA system were obtained. Experimental paramenters, such as the condition of medium, the concentration of solution and the influence of ion strength were studied for the interaction.4. The interaction between Atorvastatin calcium (AC) and BSA was investigated using electrochemical techniques in conjunction with UV absorption spectroscopy and FT-IR spectrum. Both enhancement and abatement actions of BSA on the peak current of AC were discussed in low and high BSA concentration ranges. The binding constant and binding ratio were calculated, respectively.
Keywords/Search Tags:spectroscopy, electrochemistry, drug, bovine serum albumin (BSA), interaction
PDF Full Text Request
Related items