A kind of molecularly imprinted polymer (MIPs) with high selectivity was prepared using methacrylic acid (MAA) as functional monomer, ethylene glycol dimethacrylate (EDMA) as crosslinker and Gatifloxacin as template. ...A kind of molecularly imprinted polymer (MIPs) with high selectivity was prepared using methacrylic acid (MAA) as functional monomer, ethylene glycol dimethacrylate (EDMA) as crosslinker and Gatifloxacin as template. The effect of various parameters such as volume of solvent, functional monomer dosage, crosslinker dosage and polymerization time were investigated. The selective binding experiment for substrates show that the affinity and selectivity for Gatifloxacin were higher than that for blank polymer. Scatchard analysis show that the MIPs recognized template with two kinds of binding sites. The dissociation constant Kd and maximum adsorption quantity Qmax of these two kinds of binding sites were calculated: Kd1 and Qmax1 of the binding sites with high affinity were 8.67×10-4 mol/L and 28.19μmol/g, while Kd2 and Qmax2 of the binding sites with low affinity were1.05×10-3 mol/L and 33.20μmol/g respectively.展开更多
基金China National Science Foundation (No. 20877036)Jiangsu University Science Research Funding (No. 04JDG017).
文摘A kind of molecularly imprinted polymer (MIPs) with high selectivity was prepared using methacrylic acid (MAA) as functional monomer, ethylene glycol dimethacrylate (EDMA) as crosslinker and Gatifloxacin as template. The effect of various parameters such as volume of solvent, functional monomer dosage, crosslinker dosage and polymerization time were investigated. The selective binding experiment for substrates show that the affinity and selectivity for Gatifloxacin were higher than that for blank polymer. Scatchard analysis show that the MIPs recognized template with two kinds of binding sites. The dissociation constant Kd and maximum adsorption quantity Qmax of these two kinds of binding sites were calculated: Kd1 and Qmax1 of the binding sites with high affinity were 8.67×10-4 mol/L and 28.19μmol/g, while Kd2 and Qmax2 of the binding sites with low affinity were1.05×10-3 mol/L and 33.20μmol/g respectively.
