Spectroscopic Studies On The Effects Of A Series Piperidones And Carteolol On Bovine Serum Albumin

The most abundant and important carrier plasma protein is serum albumin. It canbe widely used in conjunction with many exogenous and endogenous substances,transport and distribution, in order to maintain normal metabolism in vivo. Therefore,it pays an indispensable role in life activities. Piperidone and its derivatives have aspecial structure, that is spiroheterocyclic and its combination with some other sub-structure. Piperidone is a large class of pharmaceutical intermediates, because of itsunique multiple biological activities. Carteolol is a common treatment drug for ocularhypertension and glaucoma. So study the interaction between bovine serum albuminand them can provide some useful information for drug design and research.In this thesis, under simulated physiological conditions, the fluorescence andUV-vis spectroscopy were used to study the interaction of three series of piperidonederivatives (NBP, PPD and SPSD) and bovine serum albumin (BSA); interaction ofcarteolol hydrochloride and urea-induced bovine serum albumin. The main contentsas follows:1. Using fluorescence and UV spectroscopy to investigate the interactionbetween the N-benzyl-4-piperidone (NBP) and BSA. Data of the results describedshows that there is interaction between them at different temperatures, and the foursubstituents on the phenyl ring have a significant impact on the range of bindingconstants. By analyze the test results of the combination process of them, NBPchange the conformation of BSA;2. We have studied the interaction of BSA and PPD with the two spectrometry,verified the interaction between the two, the force to the interaction, the mechanismtype had been obtained, and also inferred the occurrence of non-radiative energytransfer;3. The effects of SPSD to BSA had been studied, in the two temperatures302and310K. After experiments, we had calculated the quenching constant ofinteraction, binding constants, binding sites and a few thermodynamic parametervalues. The results show that the substituents on the benzene ring strengthened thebinding of drug molecules to protein;4. The study results of interaction between carteolol and urea-induced BSA show that conformation of urea-induced BSA has changed in the presence of CTL.This thesis through the studies of a series of piperidone derivatives interactionwith BSA and the interaction between CTL and urea-induced BSA, provided areference data of synthetic drugs and clinical medicine. Moreover, it’s of greatimportance to the study of binding capacity of proteins under different conditions, sothat the field of protein had been enriched.