Excimer-monomer fluorescence changes by supramolecular disassembly for protein sensing and quantification

Area of Science:

• Biochemistry
• Analytical Chemistry
• Supramolecular Chemistry

Background:

• Protein quantification is crucial in biological and medical research.
• Existing methods can suffer from interference and lack specificity.
• Development of selective and robust protein sensing tools is needed.

Purpose of the Study:

• To develop a novel strategy for protein sensing and quantification.
• To utilize protein binding-induced supramolecular dissociation for detection.
• To create a probe with high selectivity and accuracy for target proteins.

Main Methods:

• Development of a supramolecular probe.
• Utilizing the ratio of monomer and excimer fluorescence for detection.
• Employing a "lock-and-key" mechanism for ligand-protein binding specificity.

Main Results:

• The developed strategy successfully senses and quantifies proteins.
• The probe exhibits excellent selectivity due to specific ligand-protein binding.
• The ratiometric approach demonstrates immunity to extrinsic quenchers.

Conclusions:

• Protein binding-induced supramolecular dissociation is an effective sensing strategy.
• The ratiometric fluorescence method provides accurate and specific protein quantification.
• This approach offers a robust tool for protein analysis in complex environments.