期刊
JOURNAL OF SEPARATION SCIENCE
卷 40, 期 15, 页码 3161-3167出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/jssc.201700456
关键词
aptamers; capillary electrophoresis; G-quadruplex; thrombin
资金
- National Natural Science Foundation [21602020, 81472450]
- Natural Science Foundation of Jiangsu Province [BK20141170]
- Project of Jiangsu Province Industry University Research joint innovation fund [BY2016029-22]
- International Scientific Cooperation Project of Changzhou Scientific Bureau [CZ20160015]
- Advanced Catalysis and Green Manufacturing Collaborative Innovation Center of Changzhou University
- 333 Project of Jiangsu Province
The dynamic binding status between the thrombin and its G-quadruplex aptamers and the stability of its interaction partners were probed using our previously established fluorescence-coupled capillary electrophoresis method. A 29-nucleic acid thrombin binding aptamer was chosen as a model to study its binding affinity with the thrombin ligand. First, the effects of the cations on the formation of G-quadruplex from unstructured 29-nucleic acid thrombin binding aptamer were examined. Second, the rapid binding kinetics between the thrombin and 6-carboxyfluorescein labeled G-quadruplex aptamer was measured. Third, the stability of G-quadruplex aptamerthrombin complex was also examined in the presence of the interfering species. Remarkably, it was found that the complementary strand of 29-nucleic acid thrombin binding aptamer could compete with G-quadruplex aptamer and thus disassociated the G-quadruplex structure into an unstructured aptamer. These data suggest that our in-house established fluorescence-coupled capillary electrophoresis assay could be applied to binding studies of the G-quadruplex aptamers, thrombin, and their ligands, while overcoming the complicated and costly approaches currently available.
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