Issue 39, 2012

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

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.

Graphical abstract: Virus-like particle nanoreactors: programmed encapsulation of the thermostable CelB glycosidase inside the P22 capsid

Supplementary files

Article information

Article type
Paper
Submitted
26 Jun 2012
Accepted
10 Aug 2012
First published
22 Aug 2012

Soft Matter, 2012,8, 10158-10166

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

D. P. Patterson, B. Schwarz, K. El-Boubbou, J. van der Oost, P. E. Prevelige and T. Douglas, Soft Matter, 2012, 8, 10158 DOI: 10.1039/C2SM26485D

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements