Study On The Interaction Of Proteins With Flavones And Their Phosphorylated Products In Solution

The research discoveries that flavones compounds have many potential pharmaceutical usages, such as their anti-oxidation,anti-virus and anti-tumor effects. The proteins are important chemical substance in our life. A number of biochemical and molecular biological investigations have revealed that proteins are frequently the targets for therapeutically active flavonoids of both natural and synthetic origin. More scientists pay attention to the study of the interaction of small molecular and protein, which are benefit to design the new factionlized medicine to surmount many difficult diseases and to development of information science.This paper is mainly to study the interactions of different structural flavones, isflavones and their phosphorylated products with protein under physiological pH by means of fluorescence and UV-Vis spectroscopy. The relationship between the structure characteristics of these compounds and binding properties of the flavonoids and protein was preliminarily discussed. The knowledge obtained of the structure features that determine the binding capacity of these compounds and protein may make us better understand the mechanics of action and pharmacological activities of them and open up new avenues for the design of the most suitable flavonoid derivatives with structural variants.The main content of this thesis is as follows:First, the interactions of flavonoids, including luteolin, apigenin, quercetin and rutin, with bovine serum albumin(BSA) were studied under physiological conditions by fluorescence spectroscopic technique. The results showed that these compounds all could form non-covalent complexes with BSA at some range of the concentration, also the number and situation of hydroxyl of the flavonoids had an important influence on the binding potency towards protein. B(3')-OH,B(4')-OH strengthened the interaction of flavonoids and BSA, but the function of C(3)-OH was reversed relatively. Besides, the interaction between flavonoids and BSA can occur only when these compounds near BSA to some extent. The extent that small molecule close to biomolecule is relate to its tridimensional volume, taking this into account, the size of...