Oligopeptide-decorated liquid crystal droplets for detecting proteases

Area of Science:

• Biochemistry
• Materials Science
• Chemical Biology

Background:

• Liquid crystals (LCs) are advanced materials with unique optical properties.
• Biomolecule-functionalized interfaces are crucial for developing sensitive biosensors.
• Protease activity is a key indicator in various biological processes and disease states.

Purpose of the Study:

• To develop novel bioactive liquid crystal (LC) droplets for protease detection.
• To functionalize LC droplets with oligopeptides for enhanced stability and specific analyte recognition.
• To investigate the LC configuration transition as a readout mechanism for protease activity.

Main Methods:

• Preparation of liquid crystal (LC) droplets stabilized by oligopeptide decoration at the LC/aqueous interface.
• Utilizing the specific enzymatic cleavage of the oligopeptide by proteases.
• Observing the transition of the internal LC configuration from bipolar to radial using microscopy.

Main Results:

• Successfully stabilized bioactive liquid crystal (LC) droplets using oligopeptide functionalization.
• Demonstrated that protease activity specifically cleaves the oligopeptide.
• Observed a distinct bipolar-to-radial transition in the LC configuration upon protease cleavage, indicating successful detection.

Conclusions:

• Oligopeptide-decorated LC droplets provide a stable and sensitive platform for protease detection.
• The observed LC configuration transition serves as a reliable indicator of protease activity.
• This approach offers a promising new strategy for developing advanced biosensing technologies.