Branched peptides for enzymatic supramolecular hydrogelation

Area of Science:

• Biomaterials science
• Supramolecular chemistry
• Enzyme catalysis

Background:

• Protease-instructed self-assembly is a growing field for creating functional soft materials.
• Existing methods often lack precise control over nanostructure formation.
• Branched peptides offer a unique structural motif not yet explored for this purpose.

Purpose of the Study:

• To demonstrate the use of branched peptides (isopeptides) as substrates for proteases.
• To generate supramolecular hydrogels through enzymatic cleavage of these branched peptides.
• To establish a new molecular strategy for protease-instructed self-assembly in soft materials.

Main Methods:

• Synthesis of branched peptides designed as protease substrates.
• Enzymatic treatment with specific proteases to cleave the peptide branches.
• Characterization of the resulting nanostructures and hydrogel formation using techniques like microscopy and rheology.

Main Results:

• Successful generation of supramolecular hydrogels from branched peptides upon enzymatic cleavage.
• Demonstration of a molecular process converting nanostructures via protease activity.
• Confirmation of a fundamentally new molecular motif for protease-instructed self-assembly.

Conclusions:

• Branched peptides serve as effective substrates for proteases to induce self-assembly into hydrogels.
• This work presents the first report of using proteases to cut branched peptides for supramolecular material generation.
• The findings introduce a novel approach for designing soft materials through enzyme-triggered molecular self-assembly.