Decorated networks of native proteins: nanomaterials with tunable mesoscopic domain size

Ioatzin Ríos de Anda, Angélique Coutable-Pennarun, Christopher Brasnett, Stephen Whitelam, Annela Seddon, John Russo, J L Ross Anderson, C Patrick Royall

Research output: Contribution to journalArticle (Academic Journal)peer-review

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Abstract

Natural and artificial proteins with designer properties and functionalities offer unparalleled opportunity for functional nanoarchitectures formed through self-assembly. However, to exploit this potential we need to design the system such that assembly results in desired architecture forms while avoiding denaturation and therefore retaining protein functionality. Here we address this challenge with a model system of fluorescent proteins. By manipulating self-assembly using techniques inspired by soft matter where interactions between the components are controlled to yield the desired structure, we have developed a methodology to assemble networks of proteins of one species which we can decorate with another, whose coverage we can tune. Consequently, the interfaces between domains of each component can also be tuned, with potential applications for example in energy - or electron - transfer. Our model system of eGFP and mCherry with tuneable interactions reveals control over domain sizes in the resulting networks.

Original languageEnglish
Number of pages11
JournalSoft Matter
Early online date30 Jun 2021
DOIs
Publication statusPublished - 7 Jul 2021

Structured keywords

  • BrisSynBio
  • Bristol BioDesign Institute

Keywords

  • Synthetic biology

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