期刊
SMALL
卷 7, 期 1, 页码 87-94出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/smll.201001428
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资金
- National Natural Science Foundation of China [20875030]
- Shuguang Project of Shanghai [07SG36]
An aptamer is a specific oligonucleotide sequence that spontaneously forms a secondary structure capable of selectively binding an analyte. An aptamer's conformation is the key to specific binding of a target molecule, even in the case of very closely related targets. Nanopores are a sensitive tool for the single-molecule analysis of DNA, peptides, and proteins transporting through the pore. Herein, a single alpha-hemolysin natural nanopore is utilized to sense the conformational changes of an adenosine 5'-triphosphate (ATP)-binding aptamer (ABA). The known DNA sequence of the ABA is used as a model to develop real-time monitoring of molecular conformational changes that occur by binding targets. The native, folded ABA structure has a nanopore unfolding time of 4.17 ms, compared with 0.29 ms for the ABA:ATP complex. A complementary 14-mer strand, which binds the ABA sequence in the key nucleic acids responsible for folding, forms linear duplex DNA, resulting in a nanopore transit time of 0.50 ms and a higher capture probability than that of the folded ABA oligomer. Competition assays between the ABA: ATP and ABA: reporter complexes are carried out, and the results suggest that the ABA: ATP complex is formed preferentially. The nanopore allows for the detection of an ABA in its folded, ATP-bound, and linear conformations.
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