Operational Condition of a Molecular Imprinting Catalyst-based Fructosyl-valine Sensor

DOI Web Site 被引用文献2件 参考文献22件
  • YAMAZAKI Tomohiko
    Biomaterial Center, National Institute for Materials Science (NIMS)
  • OHTA Shigenori
    Department of Biotechnology, Graduate School of Engineering, Tokyo University of Agriculture & Technology
  • SODE Koji
    Department of Biotechnology, Graduate School of Engineering, Tokyo University of Agriculture & Technology

抄録

We have previously reported the development of an artificial enzyme catalysing hydrolytic oxidation reaction of fructosyl-valine (Fru-val). The enzyme was prepared by molecularly imprinting a catalytic polymer composed of vinyl imidazole to form a molecular imprinting catalyst (MIC). In this study, we have attempted to improve both the selectivity and sensitivity of the MIC-based Fru-val sensor by altering the operational conditions. Assuming that the hydrophobic interaction between the valine residue of Fru-val and the cross-linker in the polymer increases with increasing ionic strength of the buffer solution, and that the hydrophilic interaction between N-epsilon-substituted fructosyl-lysine (Fru-ε-lys) and the polymer decreases, we have used a higher concentration of the buffer solution for sensor operation. The sensitivity towards Fru-val increased, whereas the sensitivity towards Fru-ε-lys decreased when a 100 mM potassium phosphate buffer was used for sensor operation instead of a 10 mM buffer. The selectivity of the MIC towards Fru-val against Fru-ε-lys increased drastically from 1.9 to 5.7. In addition, the sensor was able to measure a glycated peptide, fructosyl valyl histidyl, which is a characteristic of the N-terminal structure of glycated hemoglobin.

収録刊行物

  • Electrochemistry

    Electrochemistry 76 (8), 590-593, 2008

    公益社団法人　電気化学会

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