Decorated Protein Networks: Functional Nanomaterials with Tunable Domain Size
Ioatzin R{\i}os de Anda, Angelique Coutable-Pennarun, Chris Brasnett,, Stephen Whitelam, Annela Seddon, John Russo, J.L. Ross Anderson, and C., Patrick Royall1

TL;DR
This paper demonstrates a method to assemble fluorescent proteins into functional, tunable nanomaterials with controlled domain sizes, preserving their fluorescence and enabling customizable interfaces for potential applications like energy transfer.
Contribution
It introduces a soft matter-inspired approach to control protein self-assembly and decoration, maintaining protein functionality in nanostructures.
Findings
Proteins can be assembled into networks with tunable domain sizes.
Decorative proteins can be added with controllable coverage.
Protein functionality is preserved during assembly.
Abstract
The implementation of natural and artificial proteins with designer properties and functionalities offers unparalleled opportunity for functional nanoarchitectures formed through self-assembly. However, to exploit the opportunities offered we require the ability to control protein assembly into the desired architecture while avoiding denaturation and therefore retaining protein functionality. Here we address this challenge with a model system of fluorescent proteins. Using techniques of self-assembly manipulation inspired by soft matter where interactions between components are controlled to yield the desired structure, we show that it is possible 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 applications for example in energy transfer.…
Peer Reviews
No public reviews on file for this paper yet. If you reviewed it on a platform where reviews are public (OpenReview, ICLR, NeurIPS, ICML), you can paste yours below so the community can read it here.
Videos
No videos yet. Explain this paper in a talk, walkthrough, or lecture? Add one.
Taxonomy
TopicsBacteriophages and microbial interactions · Supramolecular Self-Assembly in Materials · Protein Structure and Dynamics
