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Ratiometric Fluorescent Pattern for Sensing Proteins Using Aqueous Polymer-Pyrene/γ-Cyclodextrin Inclusion Complexes.
1Beijing National Laboratory for Molecular Sciences; Key Laboratory of Analytical Chemistry for Living Biosystems, Institute of Chemistry, Chinese Academy of Sciences , Beijing 100190, P. R. China.
Analytical Chemistry
|January 12, 2016
Summary
A novel fluorescent sensor distinguishes proteins using polymer-pyrene/γ-cyclodextrin inclusion complex dissociation. This method offers tunable selectivity and sensitivity for protein sensing applications.
Area of Science:
- Supramolecular Chemistry
- Analytical Chemistry
- Polymer Chemistry
Background:
- Fluorescent sensors are crucial for detecting biomolecules.
- Distinguishing between different protein types remains a challenge.
- Inclusion complexes offer unique platforms for molecular recognition.
Purpose of the Study:
- To develop a ratiometric fluorescent sensor for protein detection and differentiation.
- To utilize the dissociation of polymer-pyrene/γ-cyclodextrin inclusion complexes for sensing.
- To achieve tunable selectivity and sensitivity in protein sensing.
Main Methods:
- Synthesis of aqueous polymer-pyrene via atom transfer radical polymerization.
- Formation of polymer-pyrene/γ-cyclodextrin inclusion complexes exhibiting excimer emission.
- Detection of nonmetalloproteins via inclusion complex dissociation and ratiometric fluorescence changes.
- Detection of metalloproteins via fluorescence quenching due to energy transfer.
Main Results:
- The developed inclusion complexes showed distinct responses to different proteins.
- Nonmetalloproteins induced dissociation, altering pyrene excimer/monomer emission.
- Metalloproteins quenched pyrene fluorescence via energy transfer.
- Sensor selectivity and sensitivity were tunable by altering polymer type and chain length.
Conclusions:
- A versatile and selective fluorescent platform for protein sensing was established.
- The ratiometric sensing mechanism allows for reliable protein detection.
- The tunable nature of the sensor holds promise for various protein analysis applications.

