Molecularly imprinted polymers for sample preparation: A review

Turiel, Esther; Martín‐Esteban, Antonio

doi:10.1016/j.aca.2010.04.019

Cited by 449 publications

(206 citation statements)

References 120 publications

(110 reference statements)

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“…Imprinted polymers are generated by polymerization of monomers and cross-linkers in the presence of a template [73]. The MIPs are expected to have high affinity for molecules resembling the template and can serve to extract such molecules (referred to as target molecules) from a complex mixture [74][75][76][77][78][79][80][81]. The interactions between the polymer and the target molecules are non-covalent interactions, and the affinity is largely based on the complementarity of the size, shape, electrostatics and hydrogen bonding of the MIP with the target molecule.…”

Section: Mammalian P450smentioning

confidence: 99%

Use of Chemical Auxiliaries to Control P450 Enzymes for Predictable Oxidations at Unactivated C-H Bonds of Substrates

Auclair

Polic

2015

Advances in Experimental Medicine and Biology

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Cytochrome P450 enzymes (P450s) have the ability to oxidize unactivated C-H bonds of substrates with remarkable regio-and stereoselectivity. Comparable selectivity for chemical oxidizing agents is typically difficult to achieve. Hence, there is an interest in exploiting P450s as potential biocatalysts. Despite their impressive attributes, the current use of P450s as biocatalysts is limited. While bacterial P450 enzymes typically show higher activity, they tend to be highly selective for one or a few substrates. On the other hand, mammalian P450s, especially the drugmetabolizing enzymes, display astonishing substrate promiscuity. However, product prediction continues to be challenging. This review discusses the use of small molecules for controlling P450 substrate specificity and product selectivity. The focus will be on two approaches in the area: (1) the use of decoy molecules, and (2) the application of substrate engineering to control oxidation by the enzyme.

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Section: Mammalian P450smentioning

confidence: 99%

Use of Chemical Auxiliaries to Control P450 Enzymes for Predictable Oxidations at Unactivated C-H Bonds of Substrates

Auclair

Polic

2015

Advances in Experimental Medicine and Biology

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“…Considering that the highlighted applications of MIPs as separation media have been summarized in ref. [196][197][198][199][200][201][202][203][204][205][206][207][208], more emphasis is placed here on the application of MIPs in sensors, artificial antibodies and catalysts. Table 3 summarizes the relevant studies reported [209][210][211][212][213][214][215][216][217][218][219][220][221][222][223][224][225] about applications of MIPs as separation sorbents, which are divided into four broad categories: environmental, bioanalytical, food and pharmaceutical applications.…”

Section: Highlighted Applicationsmentioning

confidence: 99%

Recent advances in molecular imprinting technology: current status, challenges and highlighted applications

2011

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Molecular imprinting technology (MIT) concerns formation of selective sites in a polymer matrix with the memory of a template. Recently, molecularly imprinted polymers (MIPs) have aroused extensive attention and been widely applied in many fields, such as solid-phase extraction, chemical sensors and artificial antibodies owing to their desired selectivity, physical robustness, thermal stability, as well as low cost and easy preparation. With the rapid development of MIT as a research hotspot, it faces a number of challenges, involving biological macromolecule imprinting, heterogeneous binding sites, template leakage, incompatibility with aqueous media, low binding capacity and slow mass transfer, which restricts its applications in various aspects. This critical review briefly reviews the current status of MIT, particular emphasis on significant progresses of novel imprinting methods, some challenges and effective strategies for MIT, and highlighted applications of MIPs. Finally, some significant attempts in further developing MIT are also proposed (236 references).

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“…Molecularly imprinted polymers (MIPs) are polymers assembled in the presence of a template. [60][61][62][63][64][65][66][67][68] After removal of the template, MIPs tend to show selective affinity for molecules containing the template moiety. This occurs mainly through noncovalent interactions such as complementarity in size, shape, electrostatics and hydrogen bonding.…”

Section: Covalent Modifications To Extend the Substrate Promiscuity Amentioning

confidence: 99%

Controlling substrate specificity and product regio- and stereo-selectivities of P450 enzymes without mutagenesis

Polic

Auclair

2014

Bioorganic & Medicinal Chemistry

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P450 enzymes (P450s) are well known for their ability to oxidize unactivated C-H bonds with high regio-and stereoselectivity. Hence, there is emerging interest in exploiting P450s as potential biocatalysts. Although bacterial P450s typically show higher activity than their mammalian counterparts, they tend to be more substrate selective. Most drug-metabolizing P450s on the other hand, display remarkable substrate promiscuity, yet product prediction remains challenging. Protein engineering is one established strategy to overcome these issues. A less explored, yet promising alternative involves substrate engineering. This review discusses the use of small molecules for controlling the substrate specificity and product selectivity of P450s. The focus is on two approaches, one taking advantage of non-covalent decoy molecules, and the other involving covalent substrate modifications

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Molecularly imprinted polymers for sample preparation: A review

Cited by 449 publications

References 120 publications

Use of Chemical Auxiliaries to Control P450 Enzymes for Predictable Oxidations at Unactivated C-H Bonds of Substrates

Use of Chemical Auxiliaries to Control P450 Enzymes for Predictable Oxidations at Unactivated C-H Bonds of Substrates

Recent advances in molecular imprinting technology: current status, challenges and highlighted applications

Controlling substrate specificity and product regio- and stereo-selectivities of P450 enzymes without mutagenesis

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