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

Authors

  • Nicholas W. Turner,

    1. Cranfield Health, Cranfield University at Silsoe, Silsoe MK45 4DT, UK
    2. Department of Bioengineering, University of Utah, Salt Lake City, Utah 84112
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  • Christopher W. Jeans,

    1. Welsh School of Pharmacy, Cardiff University, Redwood Building, King Edward VII Avenue, Cardiff CF1 3XF, UK
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  • Keith R. Brain,

    1. Welsh School of Pharmacy, Cardiff University, Redwood Building, King Edward VII Avenue, Cardiff CF1 3XF, UK
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  • Christopher J. Allender,

    1. Welsh School of Pharmacy, Cardiff University, Redwood Building, King Edward VII Avenue, Cardiff CF1 3XF, UK
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  • Vladimir Hlady,

    1. Department of Bioengineering, University of Utah, Salt Lake City, Utah 84112
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  • David W. Britt

    Corresponding author
    1. Department of Bioengineering, University of Utah, Salt Lake City, Utah 84112
    2. Department of Biological Engineering, Utah State University, 4105 Old Main Hill, Logan, Utah 84322
    • Department of Bioengineering, University of Utah, Salt Lake City, Utah 84112Ph. : (+1) 435–797-2158
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Abstract

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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