Virus-like particle nanoreactors: programmed en capsulation of the thermostable CelB glycosidase inside the P22 capsid

D.P. Patterson, B. Schwarz, K. El-Boubbou, J. van der Oost, P.E. Prevelige, T. Douglas

Research output: Contribution to journalArticleAcademicpeer-review

72 Citations (Scopus)

Abstract

Self-assembling biological systems hold great potential for the synthetic construction of new active soft nanomaterials. Here we demonstrate the hierarchical bottom-up assembly of bacteriophage P22 virus-like particles (VLPs) that encapsulate the thermostable CelB glycosidase creating catalytically active nanoreactors. The in vivo assembly and encapsulation produces P22 VLPs with a high packaging density of the tetrameric CelB, but without loss of enzyme activity or the ability of the P22 VLP to undergo unique morphological transitions that modify the VLPs internal volume and shell porosity. The P22 VLPs encapsulating CelB are also shown to retain a high percentage of the enzyme activity upon being embedded and immobilized in a polymeric matrix
Original languageEnglish
Pages (from-to)10158-10166
JournalSoft Matter
Volume8
Issue number39
DOIs
Publication statusPublished - 2012

Keywords

  • beta-glucosidase celb
  • archaeon pyrococcus-furiosus
  • protein cages
  • scaffolding protein
  • bacteriophage p22
  • silica immobilization
  • enzyme immobilization
  • gold nanoparticles
  • functional domains
  • escherichia-coli

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