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Decorating Self-Assembled Peptide Cages with Proteins

Research output: Contribution to journalArticle

Original languageEnglish
Pages (from-to)7901-7914
Number of pages14
JournalACS Nano
Volume11
Issue number8
Early online date7 Jul 2017
DOIs
DateAccepted/In press - 7 Jul 2017
DateE-pub ahead of print - 7 Jul 2017
DatePublished (current) - 22 Aug 2017

Abstract

An ability to organize and encapsulate multiple active proteins into defined objects and spaces at the nanoscale has potential applications in biotechnology, nanotechnology, and synthetic biology. Previously, we have described the design, assembly, and characterization of peptide-based self-assembled cages (SAGEs). These ≈100 nm particles comprise thousands of copies of de novo designed peptide-based hubs that array into a hexagonal network and close to give caged structures. Here, we show that, when fused to the designed peptides, various natural proteins can be co-assembled into SAGE particles. We call these constructs pSAGE for protein-SAGE. These particles tolerate the incorporation of multiple copies of folded proteins fused to either the N or the C termini of the hubs, which modeling indicates form the external and internal surfaces of the particles, respectively. Up to 15% of the hubs can be functionalized without compromising the integrity of the pSAGEs. This corresponds to hundreds of copies giving mM local concentrations of protein in the particles. Moreover, and illustrating the modularity of the SAGE system, we show that multiple different proteins can be assembled simultaneously into the same particle. As the peptide-protein fusions are made via recombinant expression of synthetic genes, we envisage that pSAGE systems could be developed modularly to actively encapsulate or to present a wide variety of functional proteins, allowing them to be developed as nanoreactors through the immobilization of enzyme cascades or as vehicles for presenting whole antigenic proteins as synthetic vaccine platforms.

    Structured keywords

  • BrisSynBio
  • Bristol BioDesign Institute

    Research areas

  • coiled coil, nanoreactor, protein cage, protein design, self-assembly, supramolecular assembly, synthetic biology

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    Rights statement: This is the author accepted manuscript (AAM). The final published version (version of record) is available online via ACS Publications at http://pubs.acs.org/doi/10.1021/acsnano.7b02368. Please refer to any applicable terms of use of the publisher.

    Accepted author manuscript, 594 KB, PDF document

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