Refine
Year of publication
Document Type
- Article (246)
- Postprint (7)
- Review (7)
- Other (2)
- Monograph/Edited Volume (1)
- Doctoral Thesis (1)
Is part of the Bibliography
- yes (264) (remove)
Keywords
- molecularly imprinted polymers (15)
- Molecularly imprinted polymers (5)
- Biosensors (4)
- Direct electron transfer (4)
- Electropolymerization (4)
- biomimetic sensors (4)
- direct electron transfer (4)
- electropolymerization (4)
- Cytochrome P450 (3)
- Molecularly imprinted polymer (3)
- bioelectrocatalysis (3)
- hydrogen peroxide (3)
- Bioelectrocatalysis (2)
- Biomimetic sensors (2)
- Cytochrome c (2)
- Epitope imprinting (2)
- Microperoxidase-11 (2)
- Nanoparticles (2)
- Proteins (2)
- Redox marker (2)
- SEIRA spectroelectrochemistry (2)
- SELEX (2)
- Scopoletin (2)
- anticancer drug (2)
- aptamers (2)
- aptasensors (2)
- biomimetic recognition elements (2)
- butyrylcholinesterase (2)
- catalysis (2)
- chemical sensors (2)
- electron transfer (2)
- electropolymerisation (2)
- enzymatic MIP synthesis (2)
- enzymatic analyte conversion (2)
- enzyme tracer (2)
- gate effect (2)
- immobilization (2)
- in vitro selection (2)
- o-phenylenediamine (2)
- redox marker (2)
- rivastigmine (2)
- self-assembled monolayer (2)
- tamoxifen (2)
- template digestion (2)
- 4-Fluoroaniline (1)
- ATP (1)
- Agrocybe aegerita peroxygenase (1)
- Aniline (1)
- Aniline biosensor (1)
- Antimalarial drug detection (1)
- Artemisinin (1)
- Au nanoparticles (1)
- Biomarker (1)
- Catalytically active MIPs (1)
- Catalytically active molecularly imprinted polymers (1)
- Catechol (1)
- Cellobiose dehydrogenase (1)
- Concanavalin A (1)
- Daptomycin (1)
- Displacement (1)
- Electro-synthesized molecularly imprinted polymer (1)
- Electrochemical sensor (1)
- Enzymatic recycling (1)
- Enzyme catalysis (1)
- Escherichia coli (1)
- Esterase (1)
- Ferritin (1)
- Ferrocene benzoboroxol biosensor (1)
- Ferrocene boronic acid (1)
- Functional scaffolds (1)
- HTHP (1)
- Hangman porphyrin (1)
- Hexokinase (1)
- Human serum albumin (1)
- Hybrid nanofilms (1)
- Hydrogen peroxide (1)
- Immobilization (1)
- Japan (1)
- Karube (1)
- MIP (1)
- Mercaptoundecanoic acid (1)
- Metalloenzymes (1)
- Microperoxidase (1)
- Microperoxidases (1)
- Molecularly Imprinted Polymers (1)
- Molecularly imprinted polymer film (1)
- Monoclonal MIPs (1)
- Multiwalled carbon nanotube (1)
- Nanohybrid (1)
- Nanostructuring (1)
- Osmium (1)
- Paracetamol (1)
- Peroxidatic activity (1)
- Personalised medicine (1)
- Personalized medicine (1)
- Phenacetin (1)
- Phenolic substances (1)
- Plastibodies (1)
- Poylaniline (1)
- Protein adsorption (1)
- Protein imprinting (1)
- Pyruvate kinase (1)
- Scopoletin (7-hydroxy-6-methoxycoumarin) (1)
- Self-assembled monolayer (1)
- Superoxide (1)
- Surface imprinting (1)
- Third generation sensor (1)
- Transferrin (1)
- Tyrosinase (1)
- Unspecific peroxygenase (1)
- Urine (1)
- acetylcholinesterase (1)
- activation of oxygen species (1)
- artificial protein binders (1)
- binding (1)
- biosensors (1)
- cancer markers (1)
- cobalt porphyrin (1)
- computationally simulated epitopes (1)
- cytochrome P450 (1)
- cytochrome c (1)
- direct electron (1)
- drug imprinting (1)
- drug sensors (1)
- electro-polymerization (1)
- electrochemical sensors (1)
- electrochemistry (1)
- electropolymers (1)
- electrosynthesis (1)
- enzymes (1)
- epitope imprinting (1)
- glycated peptide (1)
- gold (1)
- heme proteins (1)
- heterogeneous catalysis (1)
- hierarchical structures (1)
- horseradish peroxidase (1)
- lifetime achievements (1)
- modified electrodes (1)
- molecular imprinting (1)
- molecular modeling (1)
- molecularly imprinted electropolymers (1)
- molecularly imprinted polymer (1)
- monolayers (1)
- multilayer (1)
- nanoparticles (1)
- non-specific (1)
- o-Phenylenediamine (1)
- p-Aminophenol (1)
- peptide imprinting (1)
- peripheral anionic site (1)
- platinum nanoparticles (1)
- propidium (1)
- protein imprinting (1)
- protein recognition (1)
- redox gating (1)
- sulfite (1)
- sulfite oxidase (1)
- transfer (1)
Molecularly imprinted polymers (MIPs) for the recognition of proteins are expected to possess high affinity through the establishment of multiple interactions between the polymer matrix and the large number of functional groups of the target. However, while highly affine recognition sites need building blocks rich in complementary functionalities to their target, such units are likely to generate high levels of nonspecific binding. This paradox, that nature solved by evolution for biological receptors, needs to be addressed by the implementation of new concepts in molecular imprinting of proteins. Additionally, the structural variability, large size and incompatibility with a range of monomers made the development of protein MIPs to take a slow start. While the majority of MIP preparation methods are variants of chemical polymerization, the polymerization of electroactive functional monomers emerged as a particularly advantageous approach for chemical sensing application. Electropolymerization can be performed from aqueous solutions to preserve the natural conformation of the protein templates, with high spatial resolution and electrochemical control of the polymerization process. This review compiles the latest results, identifying major trends and providing an outlook on the perspectives of electrosynthesised protein-imprinted MIPs for chemical sensing. (C) 2016 Elsevier B.V. All rights reserved.
A new electrochemical MIP sensor for the most frequently used drug paracetamol (PAR) was prepared by electropolymerization of mixtures containing the template molecule and the functional monomers ophenylenediamine, resorcinol and aniline. The imprinting factor of 12 reflects the effective target binding to the MIP as compared with the non-imprinted electropolymer. Combination of the MIP with a nonspecific esterase allows the measurement of phenacetin - another analgesic drug. In the second approach the PAR containing sample solution was pretreated with tyrosinase in order to prevent electrochemical interferences by ascorbic acid and uric acid. Interference-free indication at a very low electrode potential without fouling of the electrode surface was achieved with the o-phenylenediamine: resorcinol-based MIP.
A tailor-made horseradish peroxidase (HRP) bulk composite electrode was developed on the basis of pyrolyzed cobalt tetramethoxyphenylporphyrin (CoTMPP) by modifying pore size and surface area of the porous carbon material through varying amounts of iron oxalate and sulfur prior to pyrolyzation. The materials were used to immobilize horseradish peroxidase (HRP). These electrodes were characterized in terms of their efficiency to reduce hydrogen peroxide. The heterogeneous electron transfer rate constants of different materials were determined with the rotating disk electrode method and a k(S) (401 +/- 61 s(-1)) exceeding previously reported values for native HRP was found.
Hybrid architectures which combine a MIP with an immobilized affinity ligand or a biocatalyst sum up the advantages of both components. In this paper, hybrid architectures combining a layer of a molecularly imprinted electropolymer with a mini-enzyme or a self-assembled monolayer will be presented. (i) Microperoxidase-11 (MP-11) catalyzed oxidation of the drug aminopyrine on a product-imprinted sublayer: The peroxide dependent conversion of the analyte aminopyrine takes place in the MP-11 containing layer on top of a product-imprinted electropolymer on the indicator electrode. The hierarchical architecture resulted in the elimination of interfering signals for ascorbic acid and uric acid. An advantage of the new hierarchical structure is the separation of MIP formation by electropolymerization and immobilization of the catalyst. In this way it was for the first time possible to integrate an enzyme with a MIP layer in a sensor configuration. This combination has the potential to be transferred to other enzymes, e.g. P450, opening the way to clinically important analytes. (ii) Epitope-imprinted poly-scopoletin layer for binding of the C-terminal peptide and cytochrome c (Cyt c): The MIP binds both the target peptide and the parent protein almost eight times stronger than the non-imprinted polymer with affinities in the lower micromolar range. Exchange of only one amino acid in the peptide decreases the binding by a factor of five. (iii) MUA-poly-scopoletin MIP for cytochrome c: Cyt c bound to the MIP covered gold electrode exhibits direct electron transfer with a redox potential and rate constant typical for the native protein. The MIP cover layer suppresses the displacement of the target protein by BSA or myoglobin. The combination of protein imprinted polymers with an efficient electron transfer is a new concept for characterizing electroactive proteins such as Cyt c. The competition with other proteins shows that the MIP binds its target Cyt c preferentially and that molecular shape and the charge of protein determine the binding of interfering proteins.
Conclusions and outlook
(2001)
Electrochemical immunoassays
(2000)
Operation of a miniature redox hydrogel-based pyruvate sensor in undiluted deoxygenated calf serum
(2000)
Biosensor-Stabilität
(2000)
Changing functionality of surfaces by directed self-assembly using oligonucleotides - the oligo-tag
(1999)
Natürliche Evolution hat geschaffenBiopolymereauf der Basis von Aminosäuren undNukleotidezeigt hohe chemische Selektivität und katalytische Kraft. Die molekulare Erkennung durch Antikörper und die katalytische Umwandlung der Substratmoleküle durch Enzyme findet in sogenannten Paratopen oder katalytischen Zentren des Makromoleküls statt, die typischerweise 10-15 Aminosäuren umfassen. Die konzertierte Wechselwirkung zwischen den Reaktionspartnern führt zu Affinitäten bis zu nanomolaren Konzentrationen für die Antigenbindung und nähert sich einer Million Umsätze pro Sekunde anEnzym-katalysierte Reaktionen.
Electrosynthesized molecularly imprinted polyscopoletin nanofilms for human serum albumin detection
(2017)
Molecularly imprinted polymers (MIPs) rendered selective solely by the imprinting with protein templates lacking of distinctive properties to facilitate strong target-MIP interaction are likely to exhibit medium to low template binding affinities. While this prohibits the use of such MIPs for applications requiring the assessment of very low template concentrations, their implementation for the quantification of high-abundance proteins seems to have a clear niche in the analytical practice. We investigated this opportunity by developing a polyscopoletin-based MIP nanofilm for the electrochemical determination of elevated human serum albumin (HSA) in urine. As reference for a low abundance protein ferritin-MIPs were also prepared by the same procedure. Under optimal conditions, the imprinted sensors gave a linear response to HSA in the concentration range of 20-100 mg/dm(3), and to ferritin in the range of 120-360 mg/dm(3). While as expected the obtained limit of detection was not sufficient to determine endogenous ferritin in plasma, the HSA-sensor was successfully employed to analyse urine samples of patients with albuminuria. The results suggest that MIP-based sensors may be applicable for quantifying high abundance proteins in a clinical setting. (c) 2017 Elsevier B.V. All rights reserved.
We introduce a practically generic approach for the generation of epitope-imprinted polymer-based microarrays for protein recognition on surface plasmon resonance imaging (SPRi) chips. The SPRi platform allows the subsequent rapid screening of target binding kinetics in a multiplexed and label-free manner. The versatility of such microarrays, both as synthetic and screening platform, is demonstrated through developing highly affine molecularly imprinted polymers (MIPs) for the recognition of the receptor binding domain (RBD) of SARS-CoV-2 spike protein. A characteristic nonapeptide GFNCYFPLQ from the RBD and other control peptides were microspotted onto gold SPRi chips followed by the electrosynthesis of a polyscopoletin nanofilm to generate in one step MIP arrays. A single chip screening of essential synthesis parameters, including the surface density of the template peptide and its sequence led to MIPs with dissociation constants (K-D) in the lower nanomolar range for RBD, which exceeds the affinity of RBD for its natural target, angiotensin-convertase 2 enzyme. Remarkably, the same MIPs bound SARS-CoV-2 virus like particles with even higher affinity along with excellent discrimination of influenza A (H3N2) virus. While MIPs prepared with a truncated heptapeptide template GFNCYFP showed only a slightly decreased affinity for RBD, a single mismatch in the amino acid sequence of the template, i.e. the substitution of the central cysteine with a serine, fully suppressed the RBD binding.
A nanohybrid consisting of poly(3-aminobenzenesulfonic acid-co-aniline) and multiwalled carbon nanotubes [MWCNT-P(ABS-A)]) on a gold electrode was used to immobilize the hexameric tyrosine-coordinated heme protein (HTHP). The enzyme showed direct electron transfer between the heme group of the protein and the nanostructured surface. Desorption of the noncovalently bound heme from the protein could be excluded by control measurements with adsorbed hemin on aminohexanthiol-modified electrodes. The nanostructuring and the optimised charge characteristics resulted in a higher protein coverage as compared with MUA/MU modified electrodes. The adsorbed enzyme shows catalytic activity for the cathodic H2O2 reduction and oxidation of NADH.
Simple and robust
(2021)
A spectrum of 7562 publications on Molecularly Imprinted Polymers (MIPs) has been presented in literature within the last ten years (Scopus, September 7, 2020). Around 10 % of the papers published on MIPs describe the recognition of proteins. The straightforward synthesis of MIPs is a significant advantage as compared with the preparation of enzymes or antibodies. MIPs have been synthesized from only one up to six functional monomers while proteins are made up of 20 natural amino acids. Furthermore, they can be synthesized against structures of low immunogenicity and allow multi-analyte measurements via multi-target synthesis. Electrochemical methods allow simple polymer synthesis, removal of the template and readout. Among the different sensor configurations electrochemical MIP-sensors provide the broadest spectrum of protein analytes. The sensitivity of MIP-sensors is sufficiently high for biomarkers in the sub-nanomolar region, nevertheless the cross-reactivity of highly abundant proteins in human serum is still a challenge. MIPs for proteins offer innovative tools not only for clinical and environmental analysis, but also for bioimaging, therapy and protein engineering.
Insights in electrosynthesis, target binding, and stability of peptide-imprinted polymer nanofilms
(2021)
Molecularly imprinted polymer (MIP) nanofilms have been successfully implemented for the recognition of different target molecules: however, the underlying mechanistic details remained vague.
This paper provides new insights in the preparation and binding mechanism of electrosynthesized peptide-imprinted polymer nanofilms for selective recognition of the terminal pentapeptides of the beta-chains of human adult hemoglobin, HbA, and its glycated form HbA1c.
To differentiate between peptides differing solely in a glucose adduct MIP nanofilms were prepared by a two-step hierarchical electrosynthesis that involves first the chemisorption of a cysteinyl derivative of the pentapeptide followed by electropolymerization of scopoletin.
This approach was compared with a random single-step electrosynthesis using scopo-letin/pentapeptide mixtures. Electrochemical monitoring of the peptide binding to the MIP nanofilms by means of redox probe gating revealed a superior affinity of the hierarchical approach with a Kd value of 64.6 nM towards the related target.
Changes in the electrosynthesized non-imprinted polymer and MIP nanofilms during chemical, electrochemical template removal and rebinding were substantiated in situ by monitoring the characteristic bands of both target peptides and polymer with surface enhanced infrared absorption spectroscopy.
This rational approach led to MIPs with excellent selectivity and provided key mechanistic insights with respect to electrosynthesis, rebinding and stability of the formed MIPs.