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Updated: Jul 23, 2025

Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro

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Higher-Order VLP-Based Protein Macromolecular Framework Structures Assembled via Coiled-Coil Interactions.

Nathasha D Hewagama¹, Masaki Uchida², Yang Wang¹

¹Department of Chemistry, Indiana University, 800 E Kirkwood Avenue, Bloomington, Indiana 47405, United States.

Biomacromolecules

|July 19, 2023

Summary

Researchers created a novel protein macromolecular framework (PMF) using virus-like particles (VLPs) and coiled-coil interactions. This stable, amorphous material enables efficient enzyme encapsulation for advanced biocatalysis, overcoming limitations of previous methods.

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Area of Science:

Biomimetic materials science
Supramolecular chemistry
Nanotechnology

Background:

Biological systems exhibit hierarchical organization for efficient function.
Virus-like particles (VLPs) are self-assembled, hierarchically organized structures.
VLPs can be used as building blocks for higher-order biomimetic materials.

Purpose of the Study:

To develop a versatile platform for constructing higher-order catalytic materials using P22 bacteriophage VLPs.
To overcome limitations of VLP morphology-dependent assembly in previous P22 PMF materials.
To create a stable, amorphous protein macromolecular framework (PMF) compatible with sensitive enzymes.

Main Methods:

Utilized coiled-coil peptide interactions to mediate P22 VLP interparticle assembly.
Constructed a stable, amorphous protein macromolecular framework (PMF).
Characterized the material properties of the PMF and demonstrated its use in biocatalysis.

Main Results:

Achieved P22 VLP assembly into a stable, amorphous PMF independent of VLP morphology.
Developed a PMF platform compatible with sensitive enzymes, preserving their functionality.
Constructed a 3D biocatalytic material from the disordered PMF capable of single- and multistep catalysis.

Conclusions:

Coiled-coil mediated assembly offers a versatile approach for creating higher-order protein macromolecular frameworks from VLPs.
The developed amorphous PMF is a promising platform for advanced biomimetic materials and biocatalysis.
This method enables the construction of functional catalytic materials with sensitive enzymes, expanding applications in synthetic biology and materials science.