Molecular imprinting technology: challenges and prospects for the future

Ramström, Olof; Ansell, Richard J.

doi:10.1002/(sici)1520-636x(1998)10:3<195::aid-chir1>3.0.co;2-9

Cited by 240 publications

(105 citation statements)

References 97 publications

(90 reference statements)

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“…Water is far from the ideal solvent for conventional molecular imprinting, as it competes for and disrupts potential hydrogen-bonding sites on the template and monomers (13). Any produced polymer will be required to work in conditions that are considered, in theory, unavorable to binding, such as the competition of water in binding pockets.…”

Section: Discussionmentioning

confidence: 99%

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From 3D to 2D: A Review of the Molecular Imprinting of Proteins

Turner¹,

Jeans²,

Brain³

et al. 2006

Biotechnol. Prog.

186

217

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Molecular imprinting is a generic technology that allows for the introduction of sites of specific molecular affinity into otherwise homogeneous polymeric matrices. Commonly this technique has been shown to be effective when targeting small molecules of molecular weight <1500, while extending the technique to larger molecules such as proteins has proven difficult. A number of key inherent problems in protein imprinting have been identified, including permanent entrapment, poor mass transfer, denaturation, and heterogeneity in binding pocket affinity, which have been addressed using a variety of approaches. This review focuses on protein imprinting in its various forms, ranging from conventional bulk techniques to novel thin film and monolayer surface imprinting approaches.

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Section: Discussionmentioning

confidence: 99%

“…This also limits the choice of monomers available for selection as many popular monomers are insoluble or partially soluble in water. Water is far from the ideal solvent for conventional molecular imprinting because it will compete for and potentially disrupt any hydrogen-bonding sites on the template and monomers (13).…”

Section: 24mentioning

confidence: 99%

From 3D to 2D: A Review of the Molecular Imprinting of Proteins

Turner¹,

Jeans²,

Brain³

et al. 2006

Biotechnol. Prog.

186

217

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“…9 Another factor limiting utilization of the imprinting methods designed for the small molecules is protein solubility. 6,10 The majority of the imprinting procedures are conducted in apolar, organic solvents aiming to maximize electrostatic interactions. However, poor protein solubility in apolar organic solvents makes typical imprinting procedures inappropriate toward protein imprinting.…”

Section: Introductionmentioning

confidence: 99%

Toward protein imprinting with polymer brushes

2009

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The authors described an original approach for a surface protein imprinting employing grafting of polymer brushes. Protein molecules were first chemically bound to an ultrathin ͑1-3 nm͒ poly͑glycidyl methacrylate͒ reactive polymer layer and later removed by protease treatment. Residual amino acids became grafted to the surface and to a certain extent imitated the surface chemical composition and shape of the template molecule on a nanolevel. The space surrounding the adsorbed biomolecules was modified with grafted poly͑ethylene glycol͒ layer. This led to the formation of islands of spatial nanosized pockets complementary to the protein shape. The adsorbing protein recognized the surfaces imprinted and was anchored to the substrate.

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“…Among its many applications, MIPs are a natural choice for the preparation of a solid phase with chiral cavities for the selective adsorption of enantiomers. [92][93] The most pronounced application is the design of new Chiral Stationary Phases (CSPs), mainly for High Performance Liquid Chromatographic (HPLC) applications. Most of the CSPs are non target-specific, and thus the use of molecular imprinting technologies provides the ability to tailor the solid phase for a desired enantiomer resolution.…”

Section: Resolution Of Enantiomersmentioning

confidence: 99%