Study On Interaction Between 8Q5SAC With BSA By Spectrometry Techniques

Serum albumins are the most abundant proteins in blood plasma. They are remarkably favorable for the transport, distribution and metabolism of many endogenous and exogenous ligands. BSA can combine compounds include both inorganic ions and organic compounds, such as dyes, drugs and bilirubin, etcl. We can distinguish the combining site, binding force and binding distance by means of establishing small molecules - proteins in vitro model, which not only help us understand of proteins and small molecular mechanism deeply, but also provide useful information and data for life science and guidance for the development of new drugs. In this dissertation,we describes the significance interaction of small molecules. The UV-Visible absorption spectroscopy combined with fluorescence spectroscopy, Fourier transform infrared(FT-IR) spectroscopy were employed to investigate on the the interaction of several small molecule substances with BSA on the basis of the previous researches. The present work consists of the following several parts:1. A new method for the determination of bovine serum albumin based on the quenching of synchronous fluorescence of 8Q5SAC is presented.2. The interaction between 8Q5SAC and BSA at pH=3.32 in B-R buffer conditions has been studied using fluorescence spectroscopy. The binding sites number n and binding constant K were measured by using fluorescence quenching method; The thermodynamic parameters at different temperatures indicate that hydrogen bonds and electrostatic force might play a major role in the reaction of 8Q5SAC with BSA; The distance of between donor (BSA) and acceptor (8Q5SAC) was 1.24 which can be obtained according to the F?ster non-radioactive energy transfer theory; The effect of 8Q5SAC on the conformation of BSA has been analyzed by means of synchronous fluorescence and 3D fluorescence spectra.3. The interaction between 8Q5SAC and BSA was studied by FT-IR spectroscopy in this paper. By comparing the infrared absorption of its three forms, aqueous solution, water-loss solid and pure solid. Two-dimensional (2D) map was applied to identify and compare their secondary structures. Then amideâ… and amideâ…¢curve-fitting showed that the concentration perturbation of 8Q5SAC would cause structural changes of BSA; -OH of the solution brought serious interference, while the data of water-loss solid objectively reflected the influence the interaction between 8Q5SAC and BSA in the solution made on secondary structure.