Issue 10, 2018

Tailoring lumazine synthase assemblies for bionanotechnology

Abstract

Nanoscale compartments formed by hierarchical protein self-assembly are valuable platforms for nanotechnology development. The well-defined structure and broad chemical functionality of protein cages, as well as their amenability to genetic and chemical modification, have enabled their repurposing for diverse applications. In this review, we summarize progress in the engineering of the cage-forming enzyme lumazine synthase. This bacterial nanocompartment has proven to be a malleable scaffold. The natural protein has been diversified to afford a family of unique proteinaceous capsules that have been modified, evolved and assembled with other components to produce nanoreactors, artificial organelles, delivery vehicles and virus mimics.

Graphical abstract: Tailoring lumazine synthase assemblies for bionanotechnology

Article information

Article type
Review Article
Submitted
22 feb 2018
First published
01 máj 2018

Chem. Soc. Rev., 2018,47, 3543-3557

Tailoring lumazine synthase assemblies for bionanotechnology

Y. Azuma, T. G. W. Edwardson and D. Hilvert, Chem. Soc. Rev., 2018, 47, 3543 DOI: 10.1039/C8CS00154E

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