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Programming Nanostructure Formation Through Furin-Triggered Isopeptide Conversion and Peptide Self-Assembly.

Sarah Chagri1, Jana Fetzer1, Patrick Roth1

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Macromolecular Bioscience
|October 25, 2025
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Summary
This summary is machine-generated.

Researchers designed an enzyme-responsive peptide that transforms from a kinked to a linear form, enabling the formation of nanostructures. This furin-mediated process offers potential for creating novel functional materials.

Keywords:
enzyme‐responsive peptidesfurinnanostructuresself‐assembly

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Area of Science:

  • Biomaterials Science
  • Nanotechnology
  • Chemical Biology

Background:

  • Controlled formation of synthetic nanostructures relies on precursor molecules undergoing stimulus-induced changes.
  • Enzyme-responsive systems are crucial for targeted material transformations.

Purpose of the Study:

  • To design and investigate an enzyme-responsive kinked isopeptide for controlled nanostructure formation.
  • To explore the potential of furin-mediated cleavage for triggering peptide rearrangement and self-assembly.

Main Methods:

  • Synthesis of an enzyme-responsive kinked isopeptide with a furin recognition sequence (RVRR).
  • Enzymatic cleavage assays and kinetic studies comparing with a non-cleavable control.
  • Characterization of nanostructure properties using circular dichroism, fluorescence, electron microscopy, and NMR spectroscopy.

Main Results:

  • The kinked isopeptide was successfully cleaved by furin, leading to rearrangement into a linear peptide.
  • The linear peptide self-assembled into fibrillar nanostructures.
  • Kinetics of the enzymatic transformation were elucidated.

Conclusions:

  • Furin-induced transformation of kinked isopeptides enables controlled nanostructure formation.
  • This enzyme-triggered system shows promise for designing advanced functional materials.