Controlling the Structure and Function of Protein Thin Films through Amyloid-like Aggregation

Area of Science:

• Materials Science
• Biotechnology
• Surface Chemistry

Background:

• Protein thin films (PTFs) offer versatile applications but face challenges in controlled, large-scale fabrication.
• Existing methods lack fine control over structure and function, limiting their use in advanced applications like encapsulation.

Purpose of the Study:

• To develop facile, low-cost, and green strategies for fabricating large-area PTFs with tunable structure and function.
• To explore new methods for protein assembly and functionalization for frontier research and practical applications.

Main Methods:

• Amyloid-like protein aggregation strategy for assembling proteins into large, stable 2D films.
• Chemoselective reaction-induced protein aggregation (CRIPA) using thiol-disulfide exchange reactions for controlled film formation and encapsulation.
• Modification of interfacial aggregation pathways to tailor film morphology, thickness, and porosity.

Main Results:

• Amyloid-like protein aggregation enables the formation of large-area PTFs with high interfacial adhesion.
• CRIPA allows for the encapsulation and on-demand release of functional proteins without loss of activity.
• Amyloid-inspired PTFs exhibit enhanced antimicrobial, antifouling, molecular separation, and biomineralization activities.

Conclusions:

• Developed novel strategies for protein thin film fabrication with precise control over structure and function.
• Amyloid-inspired PTFs represent a new class of biomimetic materials with significant potential in various scientific and technological fields.
• These PTFs offer a versatile platform for creating bioactive surfaces and advanced functional coatings.