分子光谱法分析某些食用合成色素及药物与蛋白结合的反应机理-molecular spectroscopic analysis of some food synthetic pigments and the reaction mechanism of drug binding with protein.docxVIP

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分子光谱法分析某些食用合成色素及药物与蛋白结合的反应机理-molecular spectroscopic analysis of some food synthetic pigments and the reaction mechanism of drug binding with protein.docx

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分子光谱法分析某些食用合成色素及药物与蛋白结合的反应机理-molecular spectroscopic analysis of some food synthetic pigments and the reaction mechanism of drug binding with protein

Abstractfluorescence of BSA could be quenched by TTZ, SY, ETS and NFLX. NFLX bound to BSA mainly by electrostatic interaction. The primary binding site for NFLX was also located atsubdomain ⅡA of BSA (site Ⅰ). In addition, the food colorants could compete with NFLXfor the binding sites from BSA. As a result, the free concentration of NFLX in blood increased, and the efficacy of the drugs changed. According to F?rster’s theory, the effects of synthetic food colorants on the binding distances (r) between drug and BSA were evaluated. Results suggested that the values of r increased due to existent of synthetic food colorants.Chapter four: The effects of synthetic food colorants on the binding reaction between ciprofloxacin hydrochloride (CPFX) and BSA were investigated by fluorescence spectroscopy. CPFX bound to BSA by electrostatic interaction. The primary binding site forCPFX was also located at subdomain ⅡA of BSA. The presence of synthetic food colorantscould alter the binding constants and distances between BSA and CPFX. The effects of colorants were dependent on their concentrations and binding affinity to BSA. The interaction could result in the change of the free, biological active fraction of CPFX in blood.Chapter five: The binding reaction between cefotaxime sodium (CTX) and chloramphenicol (CHL) with BSA at different temperatures was studied by fluorescence spectroscopy. In Tris–HCl buffer medium of pH 7.40, the quenching mechanism of the combination for BSA and drugs was a static procedure. In addition, the competitive experiments suggested that the primary binding site for both CTX and CHL was located atsite Ⅰ in sub-domain ⅡA of BSA. The fluorescence would quench to a larger degree whenCTX (or CHL) was added to the system of BSA–CHL (or BSA–CTX). Binding constants of one drug with BSA decreased when the other drug was added. Hill’s coefficients of the ternary systems were less than 1. It showed that the negative cooperativity was found when CTX and CHL bo