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Type: Artigo de periódico
Title: A Catalytically Active Molecularly Imprinted Polymer That Mimics Peroxidase Based On Hemin: Application To The Determination Of P-aminophenol.
Author: de Jesus Rodrigues Santos, Wilney
Lima, Phabyanno Rodrigues
Tarley, César Ricardo Teixeira
Kubota, Lauro Tatsuo
Abstract: Despite the increasing number of applications of molecularly imprinted polymers (MIP) in analytical chemistry, the synthesis of polymers with hemin introduced as the catalytic center to mimic the active site of peroxidase remains as a challenge. In the current work, a new type of molecularly imprinted polymer (MIP) was synthesized with 4-aminophenol (4-APh) as the template and two monomers: hemin, which acts as the catalytic center, and methacrylic acid (MAA), which is used to build the active sites. This work shows that MIP successfully mimics peroxidase. For this purpose, a flow injection analysis system coupled to an amperometric detector was investigated through multivariate analysis. The determination of 4-APh was not affected by the equimolar presence of structurally similar phenol compounds, including catechol, 4-chloro-3-methylphenol, 2-aminophenol, guaiachol, chloroguaiachol and 2-cresol, thus highlighting the good performance of the imprinted polymer. Under the optimized experimental conditions, an analytical curve covering a wide linear response range from 0.8 up to 500 micromol L(-1) (r > 0.999) was obtained, and the method gave satisfactory precisions (n = 8), as evaluated via the relative standard deviation (RSD), of 4.1 and 3.2% for solutions of 4-APh of 50 and 500 micromol L(-1), respectively. Recoveries of 96-111% from water samples (tap water and river water) spiked with 4-APh were achieved, thus illustrating the accuracy of the proposed system.
Subject: Aminophenols
Binding Sites
Biomimetic Materials
Hydrogen-ion Concentration
Molecular Structure
Reproducibility Of Results
Sensitivity And Specificity
Time Factors
Rights: fechado
Identifier DOI: 10.1007/s00216-007-1601-8
Date Issue: 2007
Appears in Collections:Unicamp - Artigos e Outros Documentos

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