2021
DOI: 10.1016/j.bios.2021.112984
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Development of glycated peptide enzyme sensor based flow injection analysis system for haemoglobin A1c monitoring using quasi-direct electron transfer type engineered fructosyl peptide oxidase

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Cited by 16 publications
(4 citation statements)
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“…The previous report was carried out using aCSF by adding human serum albumin to mimic real CSF, revealing that arPES-modified biosensing molecule works within a relevant biological fluid. Additionally, the detection of digested haemoglobin A1c using arPES-modified enzyme was also reported [15]. These reports indicate the feasibility of arPES application in the biological samples within a complex sample matrix for E-ABs.…”
Section: Discussionmentioning
confidence: 70%
See 1 more Smart Citation
“…The previous report was carried out using aCSF by adding human serum albumin to mimic real CSF, revealing that arPES-modified biosensing molecule works within a relevant biological fluid. Additionally, the detection of digested haemoglobin A1c using arPES-modified enzyme was also reported [15]. These reports indicate the feasibility of arPES application in the biological samples within a complex sample matrix for E-ABs.…”
Section: Discussionmentioning
confidence: 70%
“…The modification of redox enzymes by arPES can be achieved by a rapid and single-step conjugation, through the reaction of the N-hydroxysuccinimide ester moiety of arPES with solvent-accessible primary amine groups (e.g., Lysine residues). Thus, conjugation of arPES enabled the preparation of quasi-direct electron transfer type enzymes that do not require a mediator in solution [12][13][14][15]. Recently, we also reported the construction of a continuous glutamine sensor using arPES-modified glutamine binding protein, which undergoes a conformation change upon interaction with glutamine [16].…”
Section: Introductionmentioning
confidence: 99%
“…In addition, to prove that the FPOX-modified electrode can specifically measure FVH, significant changes in electron transfer resistance were observed after incubation of the FPOX-modified electrode with FVH, but there was no response in the control group, indicating the specific measurement of FVH. Hatada et al replaced Arg414 with Lys to form the PnFPOX (FPOX from Phaeosphaeria nodorum) N56A/R414K mutant and modified PnFPOX near FAD with amine-reactive phenazine ethosulfate (arPES), which showed quasi-direct electron transferability [106]. This electrode was combined with an enzyme flow injection analysis (FIA) system.…”
Section: Fpox Typementioning
confidence: 99%
“…FV occurs as an N-terminal unit of human HbA1c inside β-subunits (fructosyl-Val-His-Leu-Thr…) 8,9 and typically serves as a target test molecular moiety and chemical model to mimic the diagnosis of type 2 diabetes mellitus. 1,10,11 To date, an overwhelming majority of FV and related fructosyl amino acid detection methods are based on chromatography separation-mass spectrometry, 10,12 mutant proteins, 13 electrochemical biosensors, 2,9,14–18 and Pt/Au-amperometric nanomaterials 5,9,19,20 that contain the fructosyl amino-acid oxidase. These enzymatic assay systems still suffer from some drawbacks such as multiple steps for their construction, long analysis times and the requirement for specialized labs.…”
Section: Introductionmentioning
confidence: 99%