Investigation On Interaction Of Small Molecules Substances With Serum Albumin

The study of small molecules and serum albumin interaction helps tounderstand the biological macromolecular structure, unction, and derstanding of theregulatory mechanism of small moleculesof life processes, the discovery of new targetsfor prevention and treatment of disease and drug action, molecular design of drugs,mechanismof action and new drug research and development, has a very importantscientificsignificance and application value.the interaction of small molecules andmacromolecules, it is possible to truly understand the chemical nature of some of theproblems in the lifecourse. The study area has become engaged in chemistry, one of theissues of common concern of the life sciences and clinical scientists.This thesis is basedon the significanceand research trends athome and abroad to carry out small moleculeinteraction with serum albumin, on the basis of previous research, comprehensiveutilization of fluorescence spectroscopy, UV-visible absorption spectroscopy to studycertain small molecules and serum albumininteractions. This dissertation includes thefollowing sections:Chapter1: The structures, functions and natures of serum album briefly introduced.The contents and methods of interaction of different kind of small ligands withserum album reviewed.Chapter2: The interaction between Pyronine B（PB）and bovine serum album (BSA)was studied under the conditions (pH=7.4) of Tris-Hcl buffer by fluorescence spectrometry an UV-visible absorption spectroscopy. The research shows that theseinteractions result in the fluorescence quenching of BSA, which belongs to a staticquenching mechanism. The binding parameters have been evaluatedby fluorescencequenching methods. The thermodynamic parameters showed that the interactionbetween PB and BSA was mainly driven by electrostatic force. Calculated the distance of the Pyronine B and bovine serum albumin binding sites by the F rsternonradiation energy transfer theory.Chapter3: Study the interaction of the rare earth ions samarium and human serumalbumn (HSA) under the simulated physiological conditions, by fluorescencespectrometry an UV-visible absorption spectroscopy. The research shows that theseinteractions result in the fluorescence quenching of (HSA), which belongs to a staticquenching mechanism. The thermodynamic parameters showed that the interactionbetween the rare earth ions samarium and HSA was mainly driven by the van derWaals forces and hydrogen bonding.Chapter4: The interaction between XO-Sm(Ⅲ) complexes and bovine serum album(BSA) was studied under the conditions (pH=5.8) of Tris-Hcl buffer by fluorescencespectrometry an UV-visible absorption spectroscopy. The research shows that theseinteractions result in the fluorescence quenching of BSA, which belongs to mainly astatic quenching mechanism. The thermodynamic parameters showed that theinteraction between XO-Sm (Ⅲ) complexes and BSA was mainly driven byhydrophobic force. Synchronous spect rum was used to investigate the conformationalchange of BSA. between donor and acceptor was obtained from the F rster energytransfer theory.Chapter5: Conclusion and outlook.