Protein-induced low molecular weight hydrogelator self-assembly through a self-sustaining process

Area of Science:

• Materials Science
• Supramolecular Chemistry
• Biomaterials Engineering

Background:

• Controlling self-assembly is crucial for developing advanced smart materials.
• Enzyme-assisted self-assembly is a known strategy for directed self-assembly.
• Existing methods lack precise spatiotemporal control over peptide self-assemblies.

Purpose of the Study:

• To introduce a new strategy for spatiotemporal control over peptide self-assemblies.
• To utilize protein interactions to initiate and sustain self-assembly.
• To develop a method for creating supramolecular hydrogels and surface-initiated gels.

Main Methods:

• Employing a Fmoc-peptide precursor in equilibrium with a low molecular weight hydrogelator (LMWH) via a reversible disulfide bond.
• Using protein interactions to trigger the self-assembly of the hydrogelator around proteins.
• Leveraging Le Chatelier's principle to drive the continuous production of hydrogelators and self-sustaining self-assembly.

Main Results:

• Self-assembly of the hydrogelator is observed only in the presence of proteins.
• Protein interactions initiate a self-assembly process, forming hydrogelators around them.
• A self-sustaining cycle of hydrogelator production and self-assembly is established, leading to hydrogel formation in solution or surface-initiated growth on a solid support.

Conclusions:

• The protein-directed self-assembly strategy offers precise spatiotemporal control over peptide self-assemblies.
• This method enables the formation of supramolecular hydrogels in solution and surface-initiated gels.
• The approach provides a new pathway for designing smart materials with tailored self-assembly properties.