Affinity-tunable specific recognition of glycoproteins via boronate affinity-based controllable oriented surface imprinting

Wang, Shuangshou; Jin, Ye; Bie, Zijun; Liu, Zhen

doi:10.1039/c3sc52986j

Cited by 237 publications

(167 citation statements)

References 51 publications

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“…A monomer leading to more specific target-MIP interactions is the 3-aminophenylboronic acid, which is suited for the recognition of glycoproteins through the ability of the -B(OH) 2 moiety to form under alkaline conditions reversible covalent bonds with vicinal diols that are commonly found in carbohydrates [73] and glycoproteins [74]. This opportunity, although well exploited in case of chemically synthesized pAPBA MIPs [75], [76], has not been employed with electropolymerized films, which have only been prepared to date for the recognition of BSA [77], lysozyme and cytochrome c [78]; all non-glycated proteins. Wang et al imprinted pAPBA with hemoglobin, a protein that exists to a minor extent in glycated form as well, but there is no mention on the exact form of the protein [79].…”

Section: Functional Monomers For the Electrosynthesis Of Protein Mipsmentioning

confidence: 99%

“…Wang et al imprinted pAPBA with hemoglobin, a protein that exists to a minor extent in glycated form as well, but there is no mention on the exact form of the protein [79]. Future works with electrosynthesized pAPBA MIPs for glycoprotein recognition should consider prior immobilization of the template glycoprotein, which was found essential in obtaining satisfactory selectivity against other glycoproteins [76]. Beside biocompatibility, a wide variety of functional groups and extensive knowledge about the formed polymers motivated the use of dopamine [80,81] and acrylamide [57,82] for protein MIPs.…”

Section: Functional Monomers For the Electrosynthesis Of Protein Mipsmentioning

confidence: 99%

See 1 more Smart Citation

Electrosynthesized molecularly imprinted polymers for protein recognition

Erdőssy

Horváth²,

Yarman

et al. 2016

TrAC Trends in Analytical Chemistry

156

133

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Section: Functional Monomers For the Electrosynthesis Of Protein Mipsmentioning

confidence: 99%

Section: Functional Monomers For the Electrosynthesis Of Protein Mipsmentioning

confidence: 99%

Electrosynthesized molecularly imprinted polymers for protein recognition

Erdőssy

Horváth²,

Yarman

et al. 2016

TrAC Trends in Analytical Chemistry

156

133

View full text Add to dashboard Cite

“…The AFM measurements showed a thickness of 14 and 16 nm for MIPs prepared with 1 µM Trf and 10 µM Trf respectively. The thickness of the template loaded MIP films is comparable with the largest diameter of the target Trf, i.e., 13.6 nm (Wang et al, 2014). After template removal the average thickness was decreased only by 1.5 -2.8 nm, indicating that the polymer layer is resistant to the template removal procedure (Fig.…”

Section: Thickness Of the Mip Filmsmentioning

confidence: 59%

“…Following this route, Liu's group introduced UV-initiated photolithographic molecular imprinting based on boronate affinity as a general approach for the imprinting of glycoproteins (L. . The approach was further developed by using the boronic acid moiety as an affinity anchor for oriented covalent immobilization of the template prior surface imprinting (Wang et al, 2014). An approach for hierarchical imprinting of Trf was developed by Li et al (Q. Li et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

Electrosynthesized MIPs for transferrin: Plastibodies or nano-filters?

Zhang

Yarman

Erdőssy

et al. 2018

Biosensors and Bioelectronics

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Molecularly imprinted polymer (MIP) nanofilms for transferrin (Trf) have been synthesized on gold surfaces by electro-polymerizing the functional monomer scopoletin in the presence of the protein target or around pre-adsorbed Trf. As determined by atomic force microscopy (AFM) the film thickness was comparable with the molecular dimension of the target. The target (re)binding properties of the electro-synthesized MIP films was evaluated by cyclic voltammetry (CV) and square wave voltammetry (SWV) through the target-binding induced permeability changes of the MIP nanofilms to the ferricyanide redox marker, as well as by surface plasmon resonance (SPR) and surface enhanced infrared absorption spectroscopy (SEIRAS) of the immobilized protein molecules. For Trf a linear concentration dependence in the lower micromolar range and an imprinting factor of ~5 was obtained by 2 SWV and SPR. Furthermore, non-target proteins including the iron-free apo-Trf were discriminated by pronounced size and shape specificity. Whilst it is generally assumed that the rebinding of the target or of cross-reacting proteins exclusively takes place at the polymer here we considered also the interaction of the protein molecules with the underlying gold transducers. We demonstrate by SWV that adsorption of proteins suppresses the signal of the redox marker even at the bare gold surface and by SEIRAS that the treatment of the MIP with proteinase K or NaOH only partially removes the target protein. Therefore, we conclude that when interpreting binding of proteins to directly MIP-covered gold electrodes the interactions between the protein and the gold surface should also be considered.

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“…Some ten percent of MIP papers describe artificial receptors for proteins [7,[10][11][12][13], including enzymes [13][14][15][16][17][18][19][20][21]. Molecularly imprinted polymers have been mostly developed for binding of targets, thus mimicking the function of antibodies.…”

Section: Preparation Of Surface Imprinted Mipsmentioning

confidence: 99%

Enzymes as Tools in MIP-Sensors

et al. 2017

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Abstract:Molecularly imprinted polymers (MIPs) have the potential to complement antibodies in bioanalysis, are more stable under harsh conditions, and are potentially cheaper to produce. However, the affinity and especially the selectivity of MIPs are in general lower than those of their biological pendants. Enzymes are useful tools for the preparation of MIPs for both low and high-molecular weight targets: As a green alternative to the well-established methods of chemical polymerization, enzyme-initiated polymerization has been introduced and the removal of protein templates by proteases has been successfully applied. Furthermore, MIPs have been coupled with enzymes in order to enhance the analytical performance of biomimetic sensors: Enzymes have been used in MIP-sensors as "tracers" for the generation and amplification of the measuring signal. In addition, enzymatic pretreatment of an analyte can extend the analyte spectrum and eliminate interferences.

show abstract

Affinity-tunable specific recognition of glycoproteins via boronate affinity-based controllable oriented surface imprinting

Cited by 237 publications

References 51 publications

Electrosynthesized molecularly imprinted polymers for protein recognition

Electrosynthesized molecularly imprinted polymers for protein recognition

Electrosynthesized MIPs for transferrin: Plastibodies or nano-filters?

Enzymes as Tools in MIP-Sensors

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