Journal
MATERIALS
Volume 8, Issue 8, Pages 4710-4719Publisher
MDPI
DOI: 10.3390/ma8084710
Keywords
DNA aptamer; hemin; insulin; glucagon; G-quadruplex; peroxidase activity; gold electrode
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Funding
- Ministry of Education, Culture, Sports, Science and technology, Matching Fund for Private Universities [S1001013]
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We investigated an insulin-sensing method by utilizing an insulin-binding aptamer IGA3, which forms an anti-parallel G-quadruplex with folded single strands. Spectroscopic observation indicates that some anti-parallel G-quadruplex bind hemin and show peroxidase activity. In this study, the peroxidase activity of IGA3 with hemin was confirmed by spectrophotometric measurements, i.e., the activity was three-times higher than hemin itself. IGA3 was then immobilized onto a gold electrode to determine its electrochemical activity. The peroxidase activity of the immobilized IGA3-hemin complex was determined by cyclic voltammetry, and a cathodic peak current of the electrode showed a dependence on the concentration of H2O2. The cathodic peak current of the IGA3-hemin complex decreased by binding it to insulin, and this decrease depended on the concentration of insulin.
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