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This content will become publicly available on November 13, 2018

Title: Modular Self-Assembly of Protein Cage Lattices for Multistep Catalysis

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 amore » self-assembly process across multiple length scales and exhibits properties and function that arise from the interaction between individual building blocks.« less
ORCiD logo [1] ;  [1] ;  [2] ;  [2] ;  [3] ;  [4] ;  [4] ; ORCiD logo [5] ;  [1] ;  [1] ;  [6] ; ORCiD logo [7] ; ORCiD logo [1]
  1. Indiana Univ., Bloomington, IN (United States)
  2. Brookhaven National Lab. (BNL), Upton, NY (United States)
  3. Indiana Univ., Bloomington, IN (United States); Meiji Univ., Kawasaki (Japan)
  4. Montana State Univ., Bozeman, MT (United States)
  5. Univ. of Texas at Tyler, Tyler, TX (United States)
  6. Univ. of Alabama at Birmingham, Birmingham, AL (United States)
  7. Argonne National Lab. (ANL), Argonne, IL (United States)
Publication Date:
Report Number(s):
Journal ID: ISSN 1936-0851
Grant/Contract Number:
SC0012704; AC02-06CH11357
Accepted Manuscript
Journal Name:
ACS Nano
Additional Journal Information:
Journal Volume: 12; Journal Issue: 2; Journal ID: ISSN 1936-0851
American Chemical Society (ACS)
Research Org:
Brookhaven National Laboratory (BNL), Upton, NY (United States); Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org:
USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23)
Country of Publication:
United States
36 MATERIALS SCIENCE; coupled catalysis; enzyme encapsulation; hierarchical structure; nanoreactor; self-assembly; superlattice; virus-like particle
OSTI Identifier:
Alternate Identifier(s):
OSTI ID: 1460999