Modular Self-Assembly of Protein Cage Lattices for Multistep Catalysis
- Indiana Univ., Bloomington, IN (United States)
- Brookhaven National Lab. (BNL), Upton, NY (United States)
- Indiana Univ., Bloomington, IN (United States); Meiji Univ., Kawasaki (Japan)
- Montana State Univ., Bozeman, MT (United States)
- Univ. of Texas at Tyler, Tyler, TX (United States)
- Univ. of Alabama at Birmingham, Birmingham, AL (United States)
- Argonne National Lab. (ANL), Argonne, IL (United States)
The assembly of individual molecules into hierarchical structures is a promising strategy for developing three-dimensional materials with properties arising from interaction between the individual building blocks. Virus capsids are elegant examples of biomolecular nanostructures, which are themselves hierarchically assembled from a limited number of protein subunits. Here, we demonstrate the bio-inspired modular construction of materials with two levels of hierarchy: the formation of catalytically active individual virus-like particles (VLPs) through directed self-assembly of capsid subunits with enzyme encapsulation, and the assembly of these VLP building blocks into three-dimensional arrays. The structure of the assembled arrays was successfully altered from an amorphous aggregate to an ordered structure, with a face-centered cubic lattice, by modifying the exterior surface of the VLP without changing its overall morphology, to modulate interparticle interactions. The assembly behavior and resultant lattice structure was a consequence of interparticle interaction between exterior surfaces of individual particles and thus independent of the enzyme cargos encapsulated within the VLPs. These superlattice materials, composed of two populations of enzyme-packaged VLP modules, retained the coupled catalytic activity in a two-step reaction for isobutanol synthesis. As a result, this study demonstrates a significant step toward the bottom-up fabrication of functional superlattice materials using a self-assembly process across multiple length scales and exhibits properties and function that arise from the interaction between individual building blocks.
- Research Organization:
- Argonne National Lab. (ANL), Argonne, IL (United States); Brookhaven National Laboratory (BNL), Upton, NY (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23)
- Grant/Contract Number:
- AC02-06CH11357; SC0012704
- OSTI ID:
- 1435735
- Alternate ID(s):
- OSTI ID: 1460999
- Report Number(s):
- BNL--203582-2018-JAAM
- Journal Information:
- ACS Nano, Journal Name: ACS Nano Journal Issue: 2 Vol. 12; ISSN 1936-0851
- Publisher:
- American Chemical Society (ACS)Copyright Statement
- Country of Publication:
- United States
- Language:
- English
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