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Lighting Up the Pathways to Caspase Activation Using Bimolecular Fluorescence Complementation

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Caspase-3-Responsive, Fluorogenic Bivalent Bottlebrush Polymers.

Hadiqa Zafar¹, Bin Liu¹, Hung V-T Nguyen¹

¹Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States.

ACS Macro Letters

|April 22, 2024

Summary

This summary is machine-generated.

This study introduces peptide-containing bivalent bottlebrush polymers (BBPs) that release fluorescent signals when cleaved by caspase-3. BBP backbone length and linker position control enzyme accessibility and signal response.

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Area of Science:

Polymer Chemistry
Biomaterials Science
Enzyme-Responsive Materials

Background:

Designing biologically responsive materials requires controlling protease access to cleavable peptides.
Bottlebrush polymers (BBPs) offer unique architectures for precise molecular design.

Discussion:

Synthesized bivalent bottlebrush polymers (BBPs) with polyethylene glycol (PEG) and 7-amino-4-methylcoumarin (AMC) pendants.
AMC was linked via caspase-3-cleavable peptides, enabling a "turn-on" fluorescence signal upon enzymatic cleavage.
Investigated the influence of BBP backbone length and linker location on enzyme accessibility and cleavage kinetics.

Key Insights:

Enzymatic cleavage of BBPs by caspase-3 is sensitive to polymer architecture.
Backbone length and peptide-linker positioning significantly impact protease access and substrate cleavage.
Demonstrated a tunable, enzyme-responsive fluorescence system based on BBP structure.

Outlook:

Further exploration of enzyme-BBP interactions for advanced biosensors.
Potential applications in targeted drug delivery and diagnostics.
Tailoring BBP architecture for specific enzymatic responses and material functions.