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Catalytically Active MIP Architectures

Dechtrirat, Decha; Yarman, Aysu; Peng, Lei; Lettau, Kristian; Wollenberger, Ulla; Mosbach, Klaus LU and Scheller, Frieder W. (2015) In Molecularly Imprinted Catalysts: Principles, Syntheses, and Applications p.19-34
Abstract

Molecularly imprinted polymers (MIPs) have been developed mostly for the specific binding of the target, mimicking the function of antibodies. In addition to these " plastic antibodies," completely synthetic catalysts have been created that mimic substrate conversion by enzymes. In this chapter, the following examples will be presented: (1) an esterolytic MIP for phenolic esters that is prepared using a transition state analogue as a template in an abzyme mimic; (2) MIPs using metal complexes and prosthetic groups, especially heme, in enzyme mimics; (3) a new MIP-enzyme architecture combining an enzyme containing an upper layer with a product-imprinted electropolymer on an amperometric electrode. The synergistic combination of the... (More)

Molecularly imprinted polymers (MIPs) have been developed mostly for the specific binding of the target, mimicking the function of antibodies. In addition to these " plastic antibodies," completely synthetic catalysts have been created that mimic substrate conversion by enzymes. In this chapter, the following examples will be presented: (1) an esterolytic MIP for phenolic esters that is prepared using a transition state analogue as a template in an abzyme mimic; (2) MIPs using metal complexes and prosthetic groups, especially heme, in enzyme mimics; (3) a new MIP-enzyme architecture combining an enzyme containing an upper layer with a product-imprinted electropolymer on an amperometric electrode. The synergistic combination of the enzyme-catalyzed conversion of the drug aminopyrine with the MIP filter allows the interference-free measurement at a low electrode potential; and (4) protein-binding MIPs on top of a self-assembled monolayer (SAM) of an affinity ligand for the lectin concanavalin A (ConA) and the peroxidatic active hexameric tyrosine coordinated heme protein (HTHP). The oriented binding of the target protein to the SAM during formation of the MIP generates uniform binding sites. This is reflected by the high discrimination of similar lectins by the ConA-MIP and the realization of direct heterogeneous electron transfer and bioelectrocatalysis of peroxide reduction with the HTHP-MIP.

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Please use this url to cite or link to this publication:
author
organization
publishing date
type
Chapter in Book/Report/Conference proceeding
publication status
published
subject
keywords
Biomimetic catalyst, Enzyme, Enzyme mimic, Molecularly imprinted polymer
in
Molecularly Imprinted Catalysts: Principles, Syntheses, and Applications
pages
16 pages
publisher
Elsevier Inc.
external identifiers
  • Scopus:84967333743
ISBN
9780128013014
DOI
10.1016/B978-0-12-801301-4.00002-5
language
English
LU publication?
yes
id
941a057d-8cd0-4678-8a9e-f4349e0212fa
date added to LUP
2016-10-14 15:14:38
date last changed
2016-10-14 15:14:38
@misc{941a057d-8cd0-4678-8a9e-f4349e0212fa,
  abstract     = {<p>Molecularly imprinted polymers (MIPs) have been developed mostly for the specific binding of the target, mimicking the function of antibodies. In addition to these " plastic antibodies," completely synthetic catalysts have been created that mimic substrate conversion by enzymes. In this chapter, the following examples will be presented: (1) an esterolytic MIP for phenolic esters that is prepared using a transition state analogue as a template in an abzyme mimic; (2) MIPs using metal complexes and prosthetic groups, especially heme, in enzyme mimics; (3) a new MIP-enzyme architecture combining an enzyme containing an upper layer with a product-imprinted electropolymer on an amperometric electrode. The synergistic combination of the enzyme-catalyzed conversion of the drug aminopyrine with the MIP filter allows the interference-free measurement at a low electrode potential; and (4) protein-binding MIPs on top of a self-assembled monolayer (SAM) of an affinity ligand for the lectin concanavalin A (ConA) and the peroxidatic active hexameric tyrosine coordinated heme protein (HTHP). The oriented binding of the target protein to the SAM during formation of the MIP generates uniform binding sites. This is reflected by the high discrimination of similar lectins by the ConA-MIP and the realization of direct heterogeneous electron transfer and bioelectrocatalysis of peroxide reduction with the HTHP-MIP.</p>},
  author       = {Dechtrirat, Decha and Yarman, Aysu and Peng, Lei and Lettau, Kristian and Wollenberger, Ulla and Mosbach, Klaus and Scheller, Frieder W.},
  isbn         = {9780128013014},
  keyword      = {Biomimetic catalyst,Enzyme,Enzyme mimic,Molecularly imprinted polymer},
  language     = {eng},
  month        = {10},
  pages        = {19--34},
  publisher    = {ARRAY(0x94de4e0)},
  series       = {Molecularly Imprinted Catalysts: Principles, Syntheses, and Applications},
  title        = {Catalytically Active MIP Architectures},
  url          = {http://dx.doi.org/10.1016/B978-0-12-801301-4.00002-5},
  year         = {2015},
}