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BIT Research Team Makes Progress in Selective Lighting of Specific Subunits of Creatine Kinase Based on Single-molecule Rotation-limited AIE Fluorescent Probe

release date :2020-03-07 03:22:00  |   [ close window ]ViewCount:

  Beijing Institute of Technology, Mar 4th, 2020: Recently, a research team from Beijing Institute of Technology (BIT) led by Prof. Zhang Xiaoling and Prof. Zhang Rubo alongside Prof. Niu Guangle published a research paper on Angewandte Chemie International Edition, titled “In Vitro Light-Up Visualization of a Subunit-Specific Enzyme by an AIE Probe via Restriction of Single Molecular Motion”. For the first time, the paper reported an aggregation-induced luminescence (AIE) fluorescent probe that specifically recognizes creatine kinase B subunit (CK-B) based on a single-molecule motion-restricted mechanism. Imaging of CK‐B in macrophages under different stimulants including medicine, inhibitor and bacteria was also studied.

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  Isoenzymes of creatine kinase (CK-BB, CK-MM, CK-MB) are vital markers for diseases such as myocardial and cerebral infarction. As a result, the achievement in situ and dynamic isoenzyme detections are of great significance. Considering that the size of active cavity varies among different types of isoenzyme subunits, different restriction level for AIE probe to move inside the various cavities leads to a variety of fluorescent emission, which builds up the principle of high-specific detection towards isoenzymes. Based on this, the author created a new fluorescent probe TPEMA by combining the typical AIE chromophore (tetrastyrene) with creatine kinase inhibitor (ethylmalonic accid). With the help of Job plot, ITC and molecular dynamics simulation, the author proved the emission mechanism which depends solely on the special interaction between TPEMA and CK-B, and is completely different from the conventional mechanism of AIE. For the first time, the team also succeeded in dynamic fluorescence imaging analysis of CK-B within the cell on account of this highly specific response mechanism.

  Zang Tienan, a PhD student at School of Chemistry and Chemical Engineering, BIT, is the lead author of the paper. Prof. Zhang Xiaoling, Prof. Zhang Rubo and Prof. Niu Guangle from the School of Chemistry and Chemical Engineering, BIT are the corresponding authors. The research team acknowledges financial support from the General Program and the Youth Program of National Natural Science Foundation of China.

 

News Source: School of Chemistry and Chemical Engineering
Editor: News Agency of BIT
Translator: Leng Junbo, News Agency of BIT

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