Shaping Peptide Assemblies Using Multifaceted Cyclic Tectons.

Area of Science:

• Biomolecular assembly
• Nanotechnology
• Synthetic biology

Background:

• Achieving diverse nanostructures from simple building blocks under identical conditions is a challenge in synthetic biology.
• Natural systems excel at creating varied assemblies from shared modules, a feat difficult to replicate synthetically.

Purpose of the Study:

• To present a molecular scaffold-based strategy for instructing the coassembly of peptides into diverse nanostructures.
• To demonstrate control over nanostructure morphology (nanotriangles, fibrils, lamellae) using a single set of peptides.

Main Methods:

• Design and synthesis of trifaceted cyclic molecular scaffolds with addressable, orthogonal modules.
• Manipulation of dimeric coiled-coil peptides using scaffolds to control exposure of cohesive faces.
• Coassembly of peptides guided by scaffold geometry to form various dimensional nanostructures.

Main Results:

• Successfully directed the coassembly of identical peptides into distinct nanostructures including nanotriangles, fibrils, and lamellae.
• Constructed non-straight fibrils with tunable curvature by manipulating scaffold geometry.
• Demonstrated scaffold plasticity in adapting cohesive faces for different assembly morphologies.

Conclusions:

• Multifaceted cyclic scaffolds provide a reliable and predictable method for controlling biomolecular assembly.
• This approach bridges the gap between peptide building blocks and complex assemblies, offering high tunability.
• The strategy holds promise for enhancing versatility in existing biomolecular assembly systems.