Monitoring of binding of aptamer to protein by fluorescent anisotropy

Xiaokun Cai; Shunqing Xu; Zhiren Zhang; Zhiwei Liu; Wenhong Lu

doi:10.1117/12.440150

14 September 2001 Monitoring of binding of aptamer to protein by fluorescent anisotropy

Xiaokun Cai, Shunqing Xu, Zhiren Zhang, Zhiwei Liu, Wenhong Lu

Proceedings Volume 4414, International Conference on Sensor Technology (ISTC 2001); (2001) https://doi.org/10.1117/12.440150
Event: International Conference on Sensing units and Sensor Technology, 2001, Wuhan, China

Abstract

The anti-thrombin aptamer can recognize and interact with thrombin in high affinity. This interaction results in the change of the fluorescent anisotorpy in the solution of the aptamer labeled with fluorescence. We developed a new method based on the change of the fluorescent anisotropy intensity resulted from this interaction. The change in polarization was depended on the concentration of thrombin. The linear range of the determination is 0.1-100ng/ml. The detection limit for thrombin is 0.1 ng/ml. This method has been used to determine thrombin in human whole blood. Aptamer that change the fluorescence characteristics of attached fluorophore will be useful in noncompetitive fluorescence polarization assay.

Citation Download Citation

Xiaokun Cai, Shunqing Xu, Zhiren Zhang, Zhiwei Liu, and Wenhong Lu "Monitoring of binding of aptamer to protein by fluorescent anisotropy", Proc. SPIE 4414, International Conference on Sensor Technology (ISTC 2001), (14 September 2001); https://doi.org/10.1117/12.440150

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