Molecularly imprinted polymers for the recognition of proteins: The state of the art

Bossi, Alessandra Maria; Bonini, Francesca; Turner, Anthony P. F.; Piletsky, Sergey A.

doi:10.1016/j.bios.2006.06.023

Cited by 488 publications

(315 citation statements)

References 35 publications

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“…6,7 Many different targets have been imprinted including small molecules, peptides, and proteins. [8][9][10] As a result, MIPs are attractive for a wide range of applications in analytical chemistry, separation, and environmental remediation. 11,12 MIPs have been made with various types of monomers, mostly of which are acrylic and silane based.…”

Section: Introductionmentioning

confidence: 99%

Molecularly Imprinted Polymers with DNA Aptamer Fragments as Macromonomers

Zhang

Liu

2016

ACS Appl. Mater. Interfaces

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Molecularly imprinted polymers (MIPs) are produced in the presence of a template molecule. After removing the template, the cavity can selectively rebind the template. MIPs are attractive functional materials with a low cost and high stability, but traditional MIPs often suffer from low binding affinity. This study employs DNA aptamer fragments as macromonomers to improve MIPs. The DNA aptamer for adenosine was first split into two halves, fluorescently labeled, and co-polymerized into MIPs. With a fluorescence quenching assay, the importance of imprinting was confirmed. Further studies were carried out using isothermal titration calorimetry (ITC).Compared to the mixture of the free aptamer fragments, their MIPs doubled the binding affinity.Each free aptamer fragment alone cannot bind adenosine, while MIPs containing each fragment are effective binders. We further shortened one of the aptamer fragments, and the DNA length was pushed to as short as six nucleotides, yielding MIPs with a dissociation constant of 27 µM adenosine. This study provides a new method for preparing functional MIP materials by combining high affinity biopolymer fragments with low cost synthetic monomers, allowing higher binding affinity and providing a method for signaling binding based on DNA chemistry.

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Section: Introductionmentioning

confidence: 99%

Molecularly Imprinted Polymers with DNA Aptamer Fragments as Macromonomers

Zhang

Liu

2016

ACS Appl. Mater. Interfaces

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“…In general, MIPs are made with three main reaction components: cross-linking agent, functional monomer, and template molecule [2]. The template molecule is mixed with the functional monomer so that chemical bonds between the two are formed.…”

Section: Introductionmentioning

confidence: 99%

“…The cross-linking agent binds to the functional monomers upon polymerization, which embeds the template molecule in a polymer matrix. Because the functional monomers bind to the template in a specific position within the polymer, removal of the molecule in will result in an imprint with preservation of both spatial and chemical features ( Figure 1) [2][3][4][5][6]. The resulting structure of the polymer at these locations is a mirror of the template molecule that is able to preferentially rebind that molecule over competitor molecules, which do not share the same physical and chemical structure [1,2,7].…”

Section: Introductionmentioning

confidence: 99%

“…The chemical structure of proteins, with their numerous functional groups, allows many binding opportunities for a variety of functional monomers. While imprinting MIPs with protein is becoming a popular concept, many challenges, including the accessibility of binding sites, nonspecific binding, and flexible conformation of the molecules, remain in creating materials that selectively bind the desired molecules [2]. A newer method of molecular imprinting, called the epitope approach, is being explored [5].…”

Section: Introductionmentioning

confidence: 99%

“…When the original whole protein is exposed to the imprinted material, the region containing the peptide used as template can recognize its spatial and chemical mimic in the polymer ( Figure 1) [2]. In this manner, only a portion of the entire molecule is needed for preferential binding.…”

Section: Introductionmentioning

confidence: 99%

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Protein binding to peptide-imprinted porous silica scaffolds

Brown

Puleo

2008

Chemical Engineering Journal

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Of the many types of biomolecules used for molecular imprinting applications, proteins are some of the most useful, yet challenging, templates to work with. One method, termed the 'epitope approach', involves imprinting a short peptide fragment of the protein into the polymer to promote specific adsorption of the entire protein, similar to the way an antigen binds to an antibody via the epitope. Whole lysozyme or the 16 residue lysozyme C peptide was imprinted into porous silica scaffolds using sol-gel processing. After removing template, scaffolds were exposed to lysozyme and/or RNase A, which was used as a competitor molecule of comparable size. When comparing protein-to peptideimprinted scaffolds, similar amounts of lysozyme and RNase were bound from single protein solutions. However, while whole lysozyme-imprinted scaffolds showed about 4:1 preferential binding of lysozyme to RNase, peptide-imprinted scaffolds failed to show statistical significance, even though a slight preferential binding trend was present. These initial studies suggest there is potential for using peptide-imprinting to create specific protein-binding sites on porous inorganic surfaces, although further development of the materials is needed.

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Alternative and Emerging Methodologies in Ligand‐Binding Assays

Wang

Findlay

2009

Ligand‐Binding Assays

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Molecularly imprinted polymers for the recognition of proteins: The state of the art

Cited by 488 publications

References 35 publications

Molecularly Imprinted Polymers with DNA Aptamer Fragments as Macromonomers

Molecularly Imprinted Polymers with DNA Aptamer Fragments as Macromonomers

Protein binding to peptide-imprinted porous silica scaffolds

Alternative and Emerging Methodologies in Ligand‐Binding Assays

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