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The Interaction Of Co(Π), Pb(Π) And Cinnamic Acid, Sinomenine, Catechin With Bovine Serum Albumin Under The Effect Of UV C Irradiation

Posted on:2008-01-27Degree:MasterType:Thesis
Country:ChinaCandidate:H R ZhangFull Text:PDF
GTID:2144360215483319Subject:Inorganic Chemistry
Abstract/Summary:PDF Full Text Request
Chapter one: In this chapter, we summarized the structure, function, characteristic and research technique of serum albumin; the research progress of the reaction between metallic ions and serum albumin; the research progress of the reaction between medicine and serum albumin, including the mainly research and analysis content, method, and the existed deficiency in the research process between medicine and serum albumin; the content and the significance of this article were also been summarized.Chapter two: In this paper, the interaction between Co(Π), Pb(Π) and bovine serum albumin (BSA) under the effect of UV C (253.7 nm) irradiation at physiological condition have been investigated by ultraviolet-visible (UV-Vis) spectrum, ultraviolet second-derivative spectroscopy and fluorescence spectrum. The research results showed that the absorbency of BSA increased and the characteristic peaks of BSA have some shift with exposure time prolonged, which indicated that UV C irradiation make the environments of aromatic residues change. Stern-Volmer equation and Lineweaver-Burk equation showed that the fluorescence quenching of BSA by metallic ions is also a static quenching procedure and strong binding site is not change after UV C irradiation. When adding metallic ion to irradiated BSA, the binding constant (KS) decreased gradually; while irradiating the mixture of metallic ion-BSA, the binding constant (KS) increased.Chapter three: In this paper, the interaction and the energy transfer between drugs (cinnamic acid, sinomenine and catechin) and bovine serum albumin (BSA) under the effect of UV C (253.7 nm) irradiation at physiological condition have been studied by fourier transform infrared (FT-IR) spectroscopy, fluorescence quenching spectra, circular dichroism (CD) spectroscopy and raman spectrum. The binding constant, binding site and drug-binding mode were investigated, and the effect of common ions and UV C (253.7 nm) irradiation on drug-BSA system were also been studied. The results indicated that all three of drugs have the capability to static quench the fluorescence of BSA. There were similar phenomenon when all three of drugs bound with BSA: all of the binding site of the interaction between drugs and BSA is located at site ?; the protein structure is changed after binding drugs; there is non-radiation energy transfer between drugs and BSA; the acting forces are mainly a hydrogenolysis,hydrophobic binding interaction and electrostatic binding interaction; the binding constant between protein and drug was decreased after adding common ions, which means the binding force between protein and drug also decreased, thus, the common ions shortening the storage time of the drug in blood plasma and enhancing the maximum effectiveness of the drug, which is good for enhancing drug efficacy for short time clinical treatment; the binding constants are changed by UV C irradiation, which demonstrate that the influence of UV C exposure has important guiding sense on studies of the transportation and the change of function of drugs in vivo storage.
Keywords/Search Tags:metallic ion, drug, bovine serum albumin, UV C (253.7 nm), interaction, fluorescence spectrum, circular dichroism (CD) spectroscopy, FT-IR spectrum, raman spectrum
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