Study On The Interaction Between Serum Albumin,Drugs And New Fluorescence Probes With ICT Behavior

Chapter 1: The basic structure and property of protein had been introduced. The recent development of the interactions between protein and drug was described further. The property of intramolecular charge transfer and the development of determination of protein had also been reviewed. Chapter 2(1): The interactions between bendroflumethiazide (BFTZ) and human serum albumin (HSA) have been studied by fluorescence and UV-Vis spectroscopy. Binding constants for drug attachment to the various binding sites of HSA have been measured at different temperatures in physiological buffer solution. The effect of metal ions on BFTZ interaction with HSA was also investigated. The thermodynamic parameters, ΔH and ΔS, have been calculated to be 49.28KJ mol^-1>0, and 258.83J mol^-1 K^-1>0, respectively. The distance between HSA and BFTZ, r, was determined to be 1.47 nm based on Forster's non- radiative energy transfer theory. The experimental results reveal that BFTZ has a strong ability to quench the intrinsic fluorescence of HSA through a static quenching mechanism. Furthermore, the binding constants between BFTZ and HSA are remarkably independent of temperature, and decrease in the presence of various ions, usually by about 30%-55%. Hydrophobic interaction occurs between BFTZ and the sub-domain IIA of HSA.Chapter 2 ( II ) :We have studied the interaction of human serum albumin (HSA) with Hydrochorothiazide by fluorescence quenching method at different pH and temperature. The binding constants were obtained at different pH and temperature. We have also discussed the binding constants in the presence of various metal ions. According to the thermodynamic parameters the main sorts of binding force have also been obtained. The distance between HSA and Hydrochorothiazide and energy transfer efficient are determined according to the theory of energy transfer. Chapter 3: A new compound 4-(diphenylamino) biphenyl-4'-boronic acid...