A catalytically active molecularly imprinted polymer that mimics peroxidase based on hemin: application to the determination of p-aminophenol.

A catalytically active molecularly imprinted polymer that mimics peroxidase based on hemin: application to the determination of p-aminophenol. Research Abstract Details 

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A catalytically active molecularly imprinted polymer that mimics peroxidase based on hemin: application to the determination of p-aminophenol. Abstract Text:

Wilney de Jesus Rodrigues Santos,Phabyanno Rodrigues Lima, Tarley,Lauro Tatsuo Kubota,Wilney de Jesus Rodrigues Santos,Phabyanno Rodrigues Lima, Tarley,Lauro Tatsuo Kubota,Wilney de Jesus Rodrigues Santos,Phabyanno Rodrigues Lima,César Ricardo Teixeira Tarley,Lauro Tatsuo Kubota,

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.

A catalytically active molecularly imprinted polymer that mimics peroxidase based on hemin: application to the determination of p-aminophenol. Publishing Authors By Initials

W de Jesus Rodrigues Santos,PR Lima,CR Tarley,LT Kubota,W de Jesus Rodrigues Santos,PR Lima,CR Tarley,LT Kubota,W de Jesus Rodrigues Santos,PR Lima,CR Tarley,LT Kubota,

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A catalytically active molecularly imprinted polymer that mimics peroxidase based on hemin: application to the determination of p-aminophenol. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Analytical and bioanalytical chemistry

VOLUME: 389

Page Numbers: 1919-29

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ISSN: 1618-2642

DAY: 28

MONTH: 09

YEAR: 2007

A catalytically active molecularly imprinted polymer that mimics peroxidase based on hemin: application to the determination of p-aminophenol. Information

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LANGUAGE: eng

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Grant and Affiliation Information for A catalytically active molecularly imprinted polymer that mimics peroxidase based on hemin: application to the determination of p-aminophenol.

AFFILIATION: Departamento de Química Analítica, Instituto de Química, Universidade Estadual de Campinas, Campinas, SP 13084-971, Brazil.

Country: Germany

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MEDLINETA: Anal Bioanal Chem

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