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

Hierarchical organization is one of the fundamental featuresobservedin biological systems that allows for efficient and effective functioning.Virus-like particles (VLPs) are elegant examples of a hierarchicallyorganized supramolecular structure, where many subunits are self-assembledto generate the functional cage-like architecture. Utilizing VLPsas building blocks to construct two- and three-dimensional (3D) higher-orderstructures is an emerging research area in developing functional biomimeticmaterials. VLPs derived from P22 bacteriophages can be repurposedas nanoreactors by encapsulating enzymes and modular units to buildhigher-order catalytic materials via several techniques. In this study,we have used coiled-coil peptide interactions to mediate the P22 interparticleassembly into a highly stable, amorphous protein macromolecular framework(PMF) material, where the assembly does not depend on the VLP morphology,a limitation observed in previously reported P22 PMF assemblies. Manyencapsulated enzymes lose their optimum functionalities under theharsh conditions that are required for the P22 VLP morphology transitions.Therefore, the coiled-coil-based PMF provides a fitting and versatileplatform for constructing functional higher-order catalytic materialscompatible with sensitive enzymes. We have characterized the materialproperties of the PMF and utilized the disordered PMF to constructa biocatalytic 3D material performing single- and multistep catalysis.