Detection for folding of the thrombin binding aptamer using label-free electrochemical methods
Detection for folding of the thrombin binding aptamer using label-free electrochemical methods
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DOI：
10.5483/bmbrep.2008.41.2.126
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发表时间：
2008-02-29
期刊：
影响因子：
3.8
通讯作者：
Ban, Changill
中科院分区：
文献类型：
--
作者：
Cho, Minseon;Kim, Yeonwha;Ban, Changill
利用无标记电化学方法成功地检测了固定在金电极上的适体的折叠。一个凝血酶结合DNA适体被用作模型系统在各种单价阳离子的存在。阻抗谱显示，一价阳离子对适体折叠的帮助程度依次为K+ > NH4+ > Na+ > Cs+。我们的XPS分析还表明，K+和NH4+引起适体的构象变化，使其与这些单价离子形成稳定的配合物。适体与凝血酶相互作用的阻抗结果表明，凝血酶与折叠适体的相互作用大于与未折叠适体的相互作用。EQCM技术提供了这些结果的定量分析。特别是，目前的阻抗结果表明凝血酶在一定程度上参与了适体的折叠，XPS分析证实凝血酶稳定并诱导了适体的折叠。
The folding of aptamer immobilized on an Au electrode was successfully detected using label-free electrochemical methods. A thrombin binding DNA aptamer was used as a model system in the presence of various monovalent cations. Impedance spectra showed that the extent to which monovalent cations assist in folding of aptamer is ordered as K+ > NH4+ > Na+ > Cs+. Our XPS analysis also showed that K+ and NH4+ caused a conformational change of the aptamer in which it forms a stable complex with these monovalent ions. Impedance results for the interaction between aptamer and thrombin indicated that thrombin interacts more with folded aptamer than with unfolded aptamer. The EQCM technique provided a quantitative analysis of these results. In particular, the present impedance results showed that thrombin participates a folding of aptamer to some extent and XPS analysis confirmed that thrombin stabilizes and induces the folding of aptamer.