Multichannel dual protein sensing using amphiphilic supramolecular assemblies.

Area of Science:

• Supramolecular chemistry
• Biomolecular sensing
• Fluorescence spectroscopy

Background:

• Protein detection is crucial for diagnosing human diseases.
• Existing sensing methods require further refinement for specificity and sensitivity.
• Supramolecular strategies offer versatile platforms for molecular recognition.

Purpose of the Study:

• To develop a multichannel supramolecular sensing strategy for simultaneous detection of two different proteins.
• To utilize aggregation-induced emission (AIE) and related phenomena for signal amplification.
• To achieve specific protein identification through distinct fluorescence readouts.

Main Methods:

• Design of a supramolecular system capable of disassembly upon protein interaction.
• Programming protein-ligand binding or enzymatic cleavage to trigger disassembly.
• Employing two different fluorophores for multichannel signal generation.
• Utilizing aggregation-induced emission (AIE), protein-induced fluorescence enhancement (PIFE), and disassembly-induced fluorescence enhancement (DIFE) for signal readout.

Main Results:

• Demonstrated successful supramolecular disassembly induced by specific protein interactions.
• Achieved fluorescence enhancement through AIE, PIFE, and DIFE mechanisms.
• Established a multichannel readout system capable of distinguishing between two different proteins.
• Showcased the potential for specific protein sensing based on unique fluorescence signal patterns.

Conclusions:

• The developed supramolecular strategy enables sensitive and specific detection of multiple proteins.
• The multichannel readout approach enhances the reliability and accuracy of protein sensing.
• This method holds promise for applications in early disease diagnosis and biomedical research.