The Interaction Research Of Heteropolyoxometallates And Bovine Serum Albumin By Spectrometric Methods

Proteins are the direct expresser of physiological characters and the material base of life, which take on diversified physiological function. Therefore, investigating the binding mechanism of small molecules such as drugs with protein is very important in pharmacokinetics. In this dissertation, the fluorescence spectroscopy and UV-visible absorption spectroscopy were used to investigate the interaction of several heteropolyoxometallate with bovine serum albumin(BSA). It consists of four chapters:Chapter 1: The structures, functions and natures of proteins and the research of heteropolyoxometallate in pharmacodynamics were briefly introduced.Chapter 2: The interaction of Na9[SbW9O33]·19.5H2O(SbW) with BSA was studied by fluorescence method and linear sweep voltammetry under simulative physiological conditions. It was found that SbW was a strong quencher of BSA fluorescence and the quenching was static. Van der Waals interaction and hydrogen bonding were the key binding forces. The effect of pH and ionic strength on the binding constants were also studied. The synchronous fluorescence spectra revealed that the conformation of BSA was not changed in the presence of SbW.Chapter 3: Fluorescence spectroscopy and UV-visible absorption spectroscopy were employed to analyze the binding ofα-K8H2[SiW9Ti3O40]?15H2O(SiW9Ti3) to BSA. The results indicated that SiW9Ti3 binds to BSA via two types of sites and both were static quenching. Thermodynamic analysis showed that hydrophobic interaction was the main binding force in the first type of binding site and electrostatic interactions might play main role in the second type of binding sites. The conformational study showed that the conformation of BSA was changed in the presence of SiW9Ti3.Chapter 4: The interaction ofα-Na10SiW9O34?18H2O(SiW9) with BSA has been investigated by spectroscopic analysis at simulative physiological pH. It showed that SiW9 specifically binds the protein, forming a complex via a single class of binding site. The average binding distance between SiW9 and BSA was obtained and the acting force between SiW9 and BSA was mainly hydrophobic interaction. The synchronous fluorescence and UV-visible spectra showed that the conformation of BSA was changed in the presence of SiW9.