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Reference type: Journal
Authors: Kelly M, Bowen J, Gumbleton M, Allender C
Article Title: Molecularly imprinted polymers: macromolecule recognition.
Publication date: 2010
Journal: Drug Discovery Today
Volume: 15
Issue: (23-24)
Page numbers: 1112.
DOI: 10.1016/j.drudis.2010.09.435
Alternative URL: http://www.sciencedirect.com/science/article/B6T64-51902HR-2W/2/7a5bc7871a2ef4759510746454363568

Abstract: Molecular imprinting is a technique used to engineer synthetic antibody mimics by the polymerisation of so-called functional monomers and cross-linkers around a target (template) species. Following removal of the template from the polymer matrix, cavities remain which display both chemical and steric selectivity for the imprinted molecule. To date the imprinting of biologically relevant macromolecules has been somewhat unsuccessful due to the inherent complexity of imprinting such moieties in aqueous media. Unlike small, organic molecules that are typically employed as templates, macromolecular structures such as peptides and proteins can exist in a multitude of conformations which leads to the development of heterogeneous binding sites as opposed to the well defined cavities formed during the regular imprinting process. The proteins will denature in traditional imprinting environments due to the presence of organic solvents and elevated temperatures. Additionally, the size of these biomolecules means that removal from the polymer matrix and subsequent re-binding is often inefficient. As a consequence, molecular imprinting has yet to achieve its true potential as efficacious, robust, reliable and cost-effective alternatives to the currently used antibody-based recognition systems. Projects currently underway within our laboratories aim to utilise target-selective peptides, derived from a phage display library, as a high affinity 'functional monomers' in a hybrid peptide-polymer molecularly selective system. Targets include lipopolysaccharide (LPS), the major pathogenic determinant of Gram negative bacteria and prion protein which is believed to be the causative agent of a group of invariably fatal neurodegenerative diseases known as transmissible spongiform encephalopathies (TSEs). Work to date has focused on optimisation of surface chemistries. Bifunctionalised polystyrene resin and glass surfaces have been synthesised to facilitate the independent immobilisation of peptide moiety and an initiator species. Polymer growth from the surface has been monitored by Fourier transform infra-red spectroscopy and atomic force microscopy. Future work will involve optimising a number of polymerisation variables and incorporating the phage-display derived peptide into the system to fully evaluate its potential as an antibody mimic.


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