Study On The Interaction Of Some Drugs And Protein

Protein is essential to the biology of the life substances, the interactionbetween drug molecules and protein is a chemical and life science of the frontier betweentopic, it is a common concern subject in the life science, chemistry, medical circlesmany researching fields and so on. It can expound drug molecules in the animal bodytransport at the molecular level, metabolism process and function mechanism, and it canprovide the scientific basis in these. This text mainly contains the following sections.1. The interaction between buflomedil hydrochloride and trypsin has been studiedthrough fluorescence spectroscopy and UV/vis spectrophotometry.From the experimentdata, we can see that a static quenching mechanism play a main role in the fluorescencequenching process of trypsin by buflomedil hydrochloride and the F rster energy transferbetween buflomedil hydrochloride and trypsin has happened. From the thermodynamicparameter, we can see that hydrophobic interaction play a main role in the reaction. Fromthe synchronous fluorescence, we can see that the maximum emission wavelength oftryptophan and tyrosine has no shift, this fully shows that there are no significant changein the conformation of trypsin on addition of buflomedil hydrochloride.2. The interaction between potassium sodium dehydroandroan drographolidesuccinate（PSDS） and HSA has been studied through fluorescence spectroscopy.From the experiment data, we can see that the fluorescence intensity of HSA wasenhanceuud by the PSDS. At different temperatures, the binding constants of PSDS andHSA can reach104to105magnitude, it shows that the combination of the PSDS andHSA is stronger. From the thermodynamic parameters, it shows that the binding is aspontaneous process. Hydrogen bond,and van der Waals force play a main role in PSDSbinding to HSA. From the synchronous fluorescence spectra, we can see that themaximum emission wavelength of tryptophan has apparent red shift, it shows thatconformation of HSA is changed with the addition of PSDS.3. The interaction of cefuroxime sodium(CS) and bovine hemoglobin(BH b) wasinvestigated by fluorescence spectrometry, UV/vis spectrophotometry and synchronous fluorescence spctroscopy.The research showed that the fluorescence intensity of bovinehemoglobin was enhanced by cefuroxime sodium, which belongs to a static quenchingmechanism. The binding constants, thermodynamic parameters and the binding sites at290，300,310K were calculated, respectively. The hydrogen bonds and van der wallsinteractions play a main role in the binding of cefuroxime sodium with bovinehemoglobin.