Fabrication of micromagnetic beads with molecular recognition/electron-transfer peptides for the sensing of ovalbumin

Sugawara, Kazuharu; Kuramitz, Hideki; Shinohara, Hiroki

doi:10.1016/j.aca.2016.12.028

Cited by 11 publications

(8 citation statements)

References 35 publications

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“…In a previous study, we evaluated the effect of the sizes of the magnetic beads and types of cross‐linkers when the peptides were immobilized on the beads . First, peptide‐1 was immobilized on three types of beads with different diameters (AM‐40, AM‐60, and AM‐80) for use in the electrochemical measurements (Table S1).…”

Section: Resultsmentioning

confidence: 99%

“…The difference was due to the approach of oligothreonine for tyrosine‐rich peptide. When peptide‐1 was not immobilized on beads and was added alone to a solution, the value was 0.96 . This was because peptide‐1 was directly adsorbed onto the electrode surface.…”

Section: Resultsmentioning

confidence: 99%

“…When OVA sensing was performed using differential pulse voltammetry, the peak currents were decreased based on the competitive reaction to the lysozyme origin peptide by OVA and the OVA origin peptide (Figure S11). In the absence of the peptide probe, the peak currents were decreased based on binding between OVA and the lysozyme origin peptide on the beads . Because a decrease in the peak current occurred with more than 8×10 −13 M of OVA, the influence was not considered in this system.…”

Section: Resultsmentioning

confidence: 99%

“…The detection limit for OVA was 10 −12 M when OVA and the peptide probe were incubated in a solution. To improve the sensitivity of OVA measurement, lysozyme origin/electron‐transfer peptides were immobilized on magnetic beads . Since OVA was accumulated on the magnetic beads, detection at the 10 −13 M level was achieved.…”

Section: Introductionmentioning

confidence: 99%

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Electrochemical Sensing of Ovalbumin Based on the Interaction between Lysozyme Origin/Tyrosine‐rich Peptides Modified on Magnetic Beads and Oligothreonine/Ovalbumin‐origin Peptide

et al. 2019

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We developed a highly sensitive electrochemical system for the sensing of ovalbumin (OVA). Lysozyme origin/tyrosine‐rich peptides (RNRCKGTDVQAWY4C) were immobilized on magnetic beads, and the competitive reaction between OVA and oligothreonine/OVA origin peptide probe (T8VLLPDEVSG) could then be measured. In a previous study, the detection of OVA at the 10−13 M level was achieved using RNRCKGTDVQAWY4C‐modified beads via a cross‐linker. To improve the sensitivity to OVA, this system uses T8VLLPDEVSG peptide probe to measure the interaction to RNRCKGTDVQAWY4C immobilized on magnetic beads. The peak of Y4C actually was an electron‐transfer peptide, which represented the oxidation of a phenolic hydroxyl group. First, we confirmed that the oxidation response of Y4C was increased based on an improvement in the electron transfer accessibility by oligothreonine. Next, T8VLLPDEVSG peptide probe was used for the electrochemical sensing of OVA in solutions that contained consistent amounts of RNRCKGTDVQAWY4C on magnetic beads. As a result, the peak current decreased as the concentration of OVA increased. The sensitivity to OVA was improved compared with the use of only RNRCKGTDVQAWY4C on magnetic beads. The OVA detection level was 10−14 M, which approximates the results from antibody‐antigen reactions. Consequently, the proposed system is a powerful new concept in protein sensing.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Electrochemical Sensing of Ovalbumin Based on the Interaction between Lysozyme Origin/Tyrosine‐rich Peptides Modified on Magnetic Beads and Oligothreonine/Ovalbumin‐origin Peptide

et al. 2019

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“…Ovalbomin (OVA), the most common glycoprotein in egg white, has been used as a model of protein in immunoassay and allergy studies [5,6]. Thus, a series of articles have been reported about OVA assay in fetal bovine serum, human serum and eggs [7][8][9][10]. However, because of the low abundance of glycoproteins in complex biological samples and serious matrix disturbance, precise and specific analysis of these kinds of biomolecules is still a great challenge.…”

Section: Introductionmentioning

confidence: 99%

Fluorescent nanosensor designing via hybrid of carbon dots and post-imprinted polymers for the detection of ovalbumin

Wang

et al. 2020

Talanta

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We reported a facile strategy to assemble a ratiometric nanosensor for the ovalbumin (OVA) fluorescence determination and meanwhile it can be utilized for selective visual identification by naked eyes with fluorescent test papers under 365 nm UV lamp. The nanosensor was prepared through simply mixing blue color carbon dots (CDs) and green color core-shell imprinted polymers. Blue CDs were used directly as the internal reference without participating in the imprinting process and modified molecularly imprinted polymers (MIPs) were synthesized by post-imprinting, using fluorescein isothiocyanate (FITC) as fluorescence enhanced signal. Upon the addition of different concentrations of OVA, the fluorescence intensity of FITC was enhanced, while the fluorescence intensity of CDs was almost unchanged, leading to a detection limit as low as 15.4 nM. Accordingly, the fluorescence color was gradually changed from blue to dark olive green to green with naked eyes observation. Moreover, the ratiometric nanosensor was successfully applied to detect OVA in the human urine samples with satisfactory recoveries attaining of 92.0-104.0% with relative standard deviation (RSD) of 3.3-3.9% and 93.3-101.0% with RSDs of 2.7-3.8% for the spiked chicken egg white samples. This strategy reported here opens a novel pathway for biomacromolecule detection in real applications and can realize the visual observation on fluorescent test papers.

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Construction of Protein Probe with a His‐tag and an Electron‐transfer Peptide for a Target Protein Sensing

et al. 2020

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A protein probe with an electron‐transfer peptide and a His‐tag was designed to electrochemically sense a target protein. We selected tyrosine‐rich (Y4C) and tryptophan‐rich (W4C) peptides for use as electron‐transfer agents. The peak for oxidation was based on the oxidations of the phenolic hydroxy groups in Y4C and on the indole rings in W4C. Asialofetuin (ASF) with galactose residues was the protein probe, and a galactose recognition protein, soybean agglutinin (SBA), was the target protein. A protein probe composed of an amino acid and carbohydrate residue was expected to be biocompatible. When voltammetric measurements were performed using a glassy carbon electrode, the oxidation peaks of H6Y4C and ASF‐H6Y4C appeared at the same potential. The peak current of ASF‐H6Y4C was 4‐fold that of H6Y4C because of the stronger adsorption of ASF‐H6Y4C onto the electrode. The electrode response of ASF‐H6Y4C with SBA was half that of ASF‐H6Y4C alone. By contrast, the peak current of ASF‐Y4CH6 was higher than that of ASF‐H6Y4C, which was the result of a greater degree of contact between the Y4C moieties and an electrode. On the other hand, the voltammetric behaviors of ASF with W4C and a His‐tag were similar to those with Y4C and a His‐tag. The sensitivity of SBA using ASF‐Y4CH6 was at the 10−13 M level. To confirm the function of the sensing system, measurements were performed in human serum with SBA and ASF‐Y4CH6. When SBA was added, the serum had a concentration that ranged between 5.0×10−13 and 4.0×10−12 M, and the amount of SBA that could be recovered ranged from 97 to 101%. Consequently, this system could be applied to the detection of SBA in serum.

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Fabrication of micromagnetic beads with molecular recognition/electron-transfer peptides for the sensing of ovalbumin

Cited by 11 publications

References 35 publications

Electrochemical Sensing of Ovalbumin Based on the Interaction between Lysozyme Origin/Tyrosine‐rich Peptides Modified on Magnetic Beads and Oligothreonine/Ovalbumin‐origin Peptide

Electrochemical Sensing of Ovalbumin Based on the Interaction between Lysozyme Origin/Tyrosine‐rich Peptides Modified on Magnetic Beads and Oligothreonine/Ovalbumin‐origin Peptide

Fluorescent nanosensor designing via hybrid of carbon dots and post-imprinted polymers for the detection of ovalbumin

Construction of Protein Probe with a His‐tag and an Electron‐transfer Peptide for a Target Protein Sensing

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