Kubo Izumi, Eguchi Taiga
Graduate School of Engineering, Soka University, 1-236 Tangi, Hachioji, Tokyo, 192-8577, Japan.
Materials (Basel). 2015 Jul 24;8(8):4710-4719. doi: 10.3390/ma8084710.
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, , 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.
我们利用胰岛素结合适配体IGA3研究了一种胰岛素传感方法,该适配体与折叠的单链形成反平行G-四链体。光谱观察表明,一些反平行G-四链体结合血红素并表现出过氧化物酶活性。在本研究中,通过分光光度测量证实了IGA3与血红素的过氧化物酶活性,该活性比血红素本身高三倍。然后将IGA3固定在金电极上以测定其电化学活性。通过循环伏安法测定固定化的IGA3-血红素复合物的过氧化物酶活性,电极的阴极峰电流显示出对H₂O₂浓度的依赖性。IGA3-血红素复合物与胰岛素结合后阴极峰电流降低,且这种降低取决于胰岛素的浓度。