Template-Mediated Synthesis of a Polymeric Receptor Specific to Amino Acid Sequences

Klein, Jens; Whitcombe, Michael J.; Mulholland, Francis; Vulfson, Evgeny N.

doi:10.1002/(sici)1521-3773(19990712)38:13/14<2057::aid-anie2057>3.0.co;2-g

Cited by 106 publications

(49 citation statements)

References 8 publications

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“…5 Molecularly imprinted polymers 15–20 have also been employed. 21–26 Despite decades of research, however, a general method for sequence-selective binding of peptides in water remains elusive. 13,27 A notable challenge comes from the recognized difficulty in molecular recognition in water.…”

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confidence: 99%

Sequence-Selective Binding of Oligopeptides in Water through Hydrophobic Coding

2017

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A general method for sequence-specific binding of peptides remains elusive despite decades of research. By creating an array of “hydrophobically coded dimples” on the surface of a surface–core doubly cross-linked micelle, we synthesized water-soluble nanoparticle receptors to recognize peptides by the location, number, and nature of their hydrophobic side chains. Minute differences in the side chains could be distinguished and affinities up to 20 nM were obtained for biologically active oligopeptides in water.

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confidence: 99%

Sequence-Selective Binding of Oligopeptides in Water through Hydrophobic Coding

2017

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“…On the other hand, excess monomers are used in order to form template-monomer complexes, which also might cause the formation of nonselective binding sites. 102 To overcome this limitation, a semi-covalent approach was proposed, 169 also known as sacrificial spacer method, in which the template is bound covalently to a functional monomer as in the covalent approach, but the template rebinding is only based on non-covalent interactions. Because of the coupled advantages of covalent binding (strict control of functional group location and more uniform distribution) and non-covalent binding (reduced kinetic restriction during rebinding), the semi-covalent approach shows strong template binding and efficient rebinding.…”

Section: Heterogeneous Binding Sitesmentioning

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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“…Many imprinted materials indeed have been created for peptides, showing promising results for various applications. 36–41 …”

Section: Introductionmentioning

confidence: 99%

Peptide-Binding Nanoparticle Materials with Tailored Recognition Sites for Basic Peptides

Zhao

2017

Chem. Mater.

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Peptides rich in basic residues such as lysine and arginine play important roles in biology such as bacterial defense and cell penetration. Although peptide-binding materials with high sequence-specificity have broad potential applications, the diverse functionalities of peptide side chains make their molecular recognition extremely difficult. By covalently capturing micelles of a doubly cross-linkable surfactant with solubilized peptide templates, we prepared water-soluble molecularly imprinted nanoparticles with high sequence-specificity for basic peptides. The nanoparticles interact with the side chains of lysine and arginine through hydrogen bonds strengthened by the nonpolar environment of the micelle. They have hydrophobic pockets in their core complementary to the hydrophobic side chains in size and shape. These recognition sites allowed the micelles to bind basic biological peptides strongly in water, with tens to hundreds of nanomolar in binding affinity.

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Template-Mediated Synthesis of a Polymeric Receptor Specific to Amino Acid Sequences

Abstract: Polymeric receptors prepared by a combination of covalent and noncovalent imprinting show high selectivity for the amino acid sequence of the template (see schematic representation of the binding of the tripeptide Lys‐Trp‐Asp).

Cited by 106 publications

References 8 publications

Sequence-Selective Binding of Oligopeptides in Water through Hydrophobic Coding

Sequence-Selective Binding of Oligopeptides in Water through Hydrophobic Coding

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

Peptide-Binding Nanoparticle Materials with Tailored Recognition Sites for Basic Peptides

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