Evolving Emulsion Microcompartments via Enzyme-Mimicking Amyloid-Mediated Interfacial Catalysis

Area of Science:

• Soft Matter Physics
• Materials Science
• Biomimetic Chemistry

Background:

• Living organisms utilize matter and energy for metabolism and function.
• Advancements in protocell research focus on creating evolving, hierarchical microcompartments.
• Self-organization and structuration are key properties for life-like materials.

Purpose of the Study:

• To design a smart emulsion system capable of digesting substrates and driving microcompartment self-organization.
• To investigate the role of a lipase-derived peptide in amyloid fibrillation and emulsion stabilization.
• To demonstrate the formation of self-organized structures and their evolution into 3D-printable materials.

Main Methods:

• A smart emulsion system was designed using a lipase-derived peptide.
• Amyloid fibrillation of the peptide was induced to stabilize Pickering emulsions.
• Catalytic hydrolysis (organic) or mineralization (inorganic) was employed at the oil-water interface.
• High-internal phase emulsion gels were formed and characterized for 3D printing.

Main Results:

• The peptide exhibited hydrolase-like activity and stabilized emulsions.
• Emulsion microcompartments generated self-organized surfactant layers or silica scaffolds.
• Coalescence was prevented, facilitating structural evolution.
• The system successfully formed 3D-printable high-internal phase emulsion gels.

Conclusions:

• The smart emulsion system effectively digests substrates and drives self-organization.
• The developed materials mimic structural and functional aspects of living organisms.
• This work shows potential for designing self-evolving soft materials.