Biomolecular Engineering of Biosensing Molecules &amp;mdash;The Challenges in Creating Sensing Molecules for Glycated Protein Biosensing&amp;mdash;

Ferri, Stefano; Sode, Koji

doi:10.5796/electrochemistry.80.293

Cited by 9 publications

(3 citation statements)

References 39 publications

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“…As an attractive alternative to these conventional measurement systems, enzyme assay systems based on the enzyme fructosyl amino acid oxidase (FAOX) or fructosyl peptide oxidase (FPOX) have recently been commercially available. [6][7][8][9][10][11] FAOXs catalyze the oxidative degradation of fructosyl valine and/or ε-fructosyl lysine (ε-FK), which are the degradation products of HbA1c and glycated albumin, respectively ( Figure 1A). FPOXs show relatively high activity toward fructosyl valyl histidine, which corresponds to the glycosylated N-terminal dipeptide derived from HbA1c.…”

mentioning

confidence: 99%

Advancing the Development of Glycated Protein Biosensing Technology

Kameya

Sakaguchi-Mikami

Ferri

et al. 2015

J Diabetes Sci Technol

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Research advances in biochemical molecules have led to the development of convenient and reproducible biosensing molecules for glycated proteins, such as those based on the enzymes fructosyl amino acid oxidase (FAOX) or fructosyl peptide oxidase (FPOX). Recently, more attractive biosensing molecules with potential applications in next-generation biosensing of glycated proteins have been aggressively reported. We review 2 such molecules, fructosamine 6-kinase (FN6K) and fructosyl amino acid-binding protein, as well as their recent applications in the development of glycated protein biosensing systems. Research on FN6K and fructosyl amino acid-binding protein has been opening up new possibilities for the development of highly sensitive and proteolytic-digestion-free biosensing systems for glycated proteins.

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confidence: 99%

Advancing the Development of Glycated Protein Biosensing Technology

Kameya

Sakaguchi-Mikami

Ferri

et al. 2015

J Diabetes Sci Technol

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“…The FIA system was used consecutively to determine FV in more than 120 samples within 20 h. The response of the sensor to FV was five times higher than that to N ɛ -fructosyl lysine, a digestion fragment released from glycated albumin [ 88 ]. The protein engineering of FAOx was recently reviewed [ 90 ].…”

Section: Sensors For Indirect Hba1c Determination: Fructosyl Valinmentioning

confidence: 99%

Recent Progress in Electrochemical HbA1c Sensors: A Review

Wang

Anzai

2015

Materials

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This article reviews recent progress made in the development of electrochemical glycated hemoglobin (HbA1c) sensors for the diagnosis and management of diabetes mellitus. Electrochemical HbA1c sensors are divided into two categories based on the detection protocol of the sensors. The first type of sensor directly detects HbA1c by binding HbA1c on the surface of an electrode through bio-affinity of antibody and boronic acids, followed by an appropriate mode of signal transduction. In the second type of sensor, HbA1c is indirectly determined by detecting a digestion product of HbA1c, fructosyl valine (FV). Thus, the former sensors rely on the selective binding of HbA1c to the surface of the electrodes followed by electrochemical signaling in amperometric, voltammetric, impedometric, or potentiometric mode. Redox active markers, such as ferrocene derivatives and ferricyanide/ferrocyanide ions, are often used for electrochemical signaling. For the latter sensors, HbA1c must be digested in advance by proteolytic enzymes to produce the FV fragment. FV is electrochemically detected through catalytic oxidation by fructosyl amine oxidase or by selective binding to imprinted polymers. The performance characteristics of HbA1c sensors are discussed in relation to their use in the diagnosis and control of diabetic mellitus.

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“…To develop novel diagnostic kits for monitoring HbA1c or GA in patients with diabetes, our group has been engaged in the development of a variety of molecules and principles for glycated protein biosensing. These include fructosyl amino acid/peptide oxidase (FAOX/FPOX) , engineered fructosyl amino acid/peptide oxidases , molecularly imprinted polymers , and fructosyl amino acid binding proteins . Sensing systems based on FAOXs/FPOXs are commercially available and have been gradually penetrating into clinical practice because they are rapid, reproducible, and suitable for automated analyzers.…”

Section: Introductionmentioning

confidence: 99%

Electrochemical sensing system employing fructosamine 6‐kinase enables glycated albumin measurement requiring no proteolytic digestion

Kameya

Tsugawa

Yamada-Tajima

et al. 2016

Biotechnology Journal

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Currently available enzymatic methods for the measurement of glycated proteins utilize fructosyl amino acid/peptide oxidases (FAOXs/FPOXs) as sensing elements. FAOXs/FPOXs oxidize glycated amino acids or glycated dipeptides but they are not able to accept longer glycated peptides or intact glycated proteins as substrates. Therefore, pretreatment via proteolytic digestion is unavoidable with the current enzymatic methods, and there remains a need for simpler measurement methods for glycated proteins. In this study, in order to develop a novel sensing system for glycated albumin (GA), a marker for diabetes, with no requirement for proteolytic digestion, we created an electrochemical sensor based on fructosamine 6-kinase (FN6K) from Escherichia coli. Uniquely, FN6K can react directly with intact GA unlike FAOXs/FPOXs. The concentration of GA in samples was measured using a carbon-printed disposable electrode upon which FN6K as well as two additional enzymes, pyruvate kinase and pyruvate dehydrogenase were overlaid. A clear correlation between the response current and the concentration of GA was observed in the range of 20-100 µM GA, which is suitable for measurement of GA in diluted blood samples from both healthy individuals and patients with diabetes. The sensing system reported here could be applied to point-of-care-testing devices for measurement of glycated proteins.

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Biomolecular Engineering of Biosensing Molecules —The Challenges in Creating Sensing Molecules for Glycated Protein Biosensing—

Cited by 9 publications

References 39 publications

Advancing the Development of Glycated Protein Biosensing Technology

Advancing the Development of Glycated Protein Biosensing Technology

Recent Progress in Electrochemical HbA1c Sensors: A Review

Electrochemical sensing system employing fructosamine 6‐kinase enables glycated albumin measurement requiring no proteolytic digestion

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