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Studies on the Interactions between Drugs and Proteins in Physiological Solution by Spectral Methods

Author: JinFen
Tutor: LvJianQuan
School: Central China Normal University
Course: Analytical Chemistry
Keywords: Interaction Protein Drugs Fluorescence spectroscopy Circular dichroism spectra
CLC: R96
Type: Master's thesis
Year: 2007
Downloads: 261
Quote: 4
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Abstract


In this thesis, respectively by UV - visible absorption spectroscopy, fluorescence spectroscopy, circular dichroism spectroscopy as a research tool to study drug, drug - protein interactions of metal complexes with biological macromolecules. This document is divided into four chapters, each chapter is summarized below. Chapter overview of small drug molecules, the means of the study of the interaction of metal ions and their complexes with biological macromolecules, based on research content, thinking of elevation title of this paper. Chapter II study using fluorescence spectroscopy, UV - visible absorption spectroscopy and circular dichroism spectroscopy under physiological conditions lomefloxacin - copper ions (LMF-Cu 2 ) and bovine serum albumin (BSA ) of the binding reaction. Lomefloxacin Lomefloxacin - Copper bovine serum albumin strong fluorescence quenching effect Lomefloxacin Lomefloxacin - copper fluorescence emission spectra of UV absorption spectra and bovine serum albumin with a certain degree of overlap , which was lomefloxacin lomefloxacin - copper ion with bovine serum albumin binding constant of the reaction, the number of binding sites and binding distance lomefloxacin lomefloxacin - copper ions and bovine serum albumin (BSA respectively), enthalpy and entropy changes for of-7.970kJ mol -1 and47.438J mol -1 K -1 -12.469kJ mol -1 and 33.542J mol -1 K -1 , indicating that electrostatic forces play a major role in the two systems. Synchronous fluorescence spectroscopy, three-dimensional fluorescence spectroscopy, circular dichroism spectra can be inferred that affect the conformation of lomefloxacin lomefloxacin - Copper bovine serum albumin, copper ions enhance lomefloxacin and bovine serum albumin binding reaction. Chapter III using a variety of spectroscopic techniques to study the physiological conditions lomefloxacin - copper ion (LMF-Cu 2 ) and human serum albumin (HSA) interactions and thermodynamic characteristics. The experiments show that the lomefloxacin lomefloxacin - copper with human serum albumin strong binding effect and fluorescence quenching was static quenching. Lomefloxacin lomefloxacin - of copper with human serum albumin binding constant of the binding reaction, the number of binding sites were 4.924 × 10 5 L mol -1 / 1.473,8.990 × 10 4 Lmol -1 / 1.785, thermodynamic parameters ΔH, ΔS were of-2.189kJ mol -1 / 61.25J mol -1 K -1 ,-7.401kJ mol -1 and 47.63J mol -1 K -1 , the interaction force as static electricity, measured according to Forster's non-radiative energy transfer mechanism combined distance 5.006nm and 4.709nm. Synchronous fluorescence spectroscopy, three-dimensional fluorescence spectroscopy, circular dichroism spectra investigated the conformational change of human serum albumin. Chapter thionine studied by fluorescence spectroscopy with bovine serum albumin (BSA) interactions. The results show that: thionine strong quenching effect on the fluorescence of bovine serum albumin, fluorescence quenching was static quenching process, and its mechanism is a mechanism of energy transfer. The results obtained from fluorescence quenching the reaction at different temperatures the binding constant K, K-value decreased with the reaction temperature rose. By the reaction enthalpy change, entropy change, and the combination of them is static electricity. Based on the non-radiative energy transfer mechanism, the combination of location and the efficiency of energy transfer was obtained.

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