Shaping Protein Amphiphilic Assemblies via Allosteric Effect: From 1D Nanofilament to 2D Rectangular Nanosheet

Area of Science:

• Biomaterials Science
• Protein Engineering
• Nanotechnology

Background:

• Shaping protein assemblies into specific nanostructures is a significant challenge in materials science.
• Existing methods often lack dynamic control over the self-assembly process.

Purpose of the Study:

• To introduce a novel strategy for the dynamic manipulation of protein amphiphilic self-assembly.
• To demonstrate the use of allosteric regulation for precise control over protein nanostructure formation.

Main Methods:

• Exploiting the allosteric effect of proteins to induce conformational changes.
• Utilizing adenylate kinase (AKe) as an allosteric protein to create protein amphiphiles.
• Tuning the allosteric signal level to control protein conformational folding and unfolding.

Main Results:

• Adenylate kinase-based protein amphiphiles demonstrated transformation between 1D nanofilaments and 2D crystalline nanosheets.
• The degree of allosteric control allowed for molding protein nanostructures into various morphologies and dimensionalities.
• The strategy proved to be universal for constructing dynamic protein structural materials.

Conclusions:

• Allosteric regulation offers a powerful tool for flexibly manipulating protein self-assembly.
• This method enables the creation of dynamic protein nanostructures with tunable architectures.
• The approach opens new avenues for developing advanced protein-based structural materials.