Precisely controlled molecular imprinting of glutathione-s-transferase by orientated template immobilization using specific interaction with an anchored ligand on a gold substrate

Kamon, Yuri; Matsuura, Ryo; Kitayama, Yukiya; Ooya, Tooru; Takeuchi, Toshio

doi:10.1039/c4py00350k

Cited by 49 publications

(39 citation statements)

References 46 publications

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“…before formation of the imprinted layer. Template molecules can be immobilized on the surface via either reversible covalent bonding (like imine bond and phenylboronic acid ester), or affinity interactions such as those based on an enzyme and its inhibitor [10][11][12][13][14]. Also, the template proteins can be physically adsorbed on the surface of the supports modified with suitable functional groups [15][16][17][18][19].…”

Section: Introductionmentioning

confidence: 99%

Enhanced surface imprinting of lysozyme over a new kind of magnetic chitosan submicrospheres

Guo

Yuan

2015

Journal of Colloid and Interface Science

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Section: Introductionmentioning

confidence: 99%

Enhanced surface imprinting of lysozyme over a new kind of magnetic chitosan submicrospheres

Guo

Yuan

2015

Journal of Colloid and Interface Science

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“…The layers were fabricated by surface-initiated activators generated by electron transfer for atom transfer radical polymerization (AGET ATRP), [27][28][29][30][31][32][33][34][35][36] where the properties were modulated by changing polymerization time and initiator density at the surface (Scheme 1). The layers were fabricated by surface-initiated activators generated by electron transfer for atom transfer radical polymerization (AGET ATRP), [27][28][29][30][31][32][33][34][35][36] where the properties were modulated by changing polymerization time and initiator density at the surface (Scheme 1).…”

Section: Introductionmentioning

confidence: 99%

Synthesis of grafted phosphorylcholine polymer layers as specific recognition ligands for C-reactive protein focused on grafting density and thickness to achieve highly sensitive detection

Kamon

Kitayama

Itakura

et al. 2015

Phys. Chem. Chem. Phys.

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We studied the effects of layer thickness and grafting density of poly(2-methacryloyloxyethyl phosphorylcholine) (PMPC) thin layers as specific ligands for the highly sensitive binding of C-reactive protein (CRP). PMPC layer thickness was controlled by surface-initiated activators generated by electron transfer for atom transfer radical polymerization (AGET ATRP). PMPC grafting density was controlled by utilizing mixed self-assembled monolayers with different incorporation ratios of the bis[2-(2-bromoisobutyryloxy)undecyl] disulfide ATRP initiator, as modulated by altering the feed molar ratio with (11-mercaptoundecyl)tetra(ethylene glycol). X-ray photoelectron spectroscopy and ellipsometry measurements were used to characterize the modified surfaces. PMPC grafting densities were estimated from polymer thickness and the molecular weight obtained from sacrificial initiator during surface-initiated AGET ATRP. The effects of thickness and grafting density of the obtained PMPC layers on CRP binding performance were investigated using surface plasmon resonance employing a 10 mM Tris-HCl running buffer containing 140 mM NaCl and 2 mM CaCl2 (pH 7.4). Furthermore, the non-specific binding properties of the obtained layers were investigated using human serum albumin (HSA) as a reference protein. The PMPC layer which has 4.6 nm of thickness and 1.27 chains per nm(2) of grafting density showed highly sensitive CRP detection (limit of detection: 4.4 ng mL(-1)) with low non-specific HSA adsorption, which was improved 10 times than our previous report of 50 ng mL(-1).

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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.

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Precisely controlled molecular imprinting of glutathione-s-transferase by orientated template immobilization using specific interaction with an anchored ligand on a gold substrate

Abstract: We demonstrate a novel synthetic route for molecularly imprinted polymer (MIP) thin films using a bottom-up approach utilizing protein–ligand specific interactions.

Cited by 49 publications

References 46 publications

Enhanced surface imprinting of lysozyme over a new kind of magnetic chitosan submicrospheres

Enhanced surface imprinting of lysozyme over a new kind of magnetic chitosan submicrospheres

Synthesis of grafted phosphorylcholine polymer layers as specific recognition ligands for C-reactive protein focused on grafting density and thickness to achieve highly sensitive detection

Enzymes as Tools in MIP-Sensors

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